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Methylenetetrahydrofolate reductase (EC 1.5.1.20)

 MTHR_HUMAN              Reviewed;         656 AA.
P42898; B2R7A6; Q5SNW6; Q5SNW9; Q7Z6M6; Q8IU73; Q9UQR2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 3.
18-JUL-2018, entry version 180.
RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000305};
EC=1.5.1.20 {ECO:0000269|PubMed:25736335};
Name=MTHFR;
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).
Rozen R., Goyette P.;
"cDNA for human methylenetetrahydrofolate reductase.";
Patent number WO9533054, 07-DEC-1995.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9680386; DOI=10.1007/s003359900838;
Goyette P., Pai A., Milos R., Frosst P., Tran P., Chen Z., Chan M.,
Rozen R.;
"Gene structure of human and mouse methylenetetrahydrofolate reductase
(MTHFR).";
Mamm. Genome 9:652-656(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Homberger A., Linnebank M., Winter C., Rapp B., Koch H.G.;
"Revised translation initiation site of the human
methylenetetrahydrofolate reductase (MTHFR).";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-222.
TISSUE=Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-68; VAL-222;
ARG-422; ALA-429; CYS-519; GLN-594 AND MET-653.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-594.
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-415 (ISOFORM 1), AND VARIANT
HOMOCYSTINURIA GLN-157.
TISSUE=Liver;
PubMed=7920641; DOI=10.1038/ng0694-195;
Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S.,
Matthews R.G., Rozen R.;
"Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping
and mutation identification.";
Nat. Genet. 7:195-200(1994).
[10]
ERRATUM.
PubMed=7951330;
Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S.,
Matthews R.G., Rozen R.;
Nat. Genet. 7:551-551(1994).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-71 (ISOFORM 2), AND
ALTERNATIVE SPLICING.
PubMed=12370778; DOI=10.1007/s00335-002-2167-6;
Tran P., Leclerc D., Chan M., Pai A., Hiou-Tim F., Wu Q., Goyette P.,
Artigas C., Milos R., Rozen R.;
"Multiple transcription start sites and alternative splicing in the
methylenetetrahydrofolate reductase gene result in two enzyme
isoforms.";
Mamm. Genome 13:483-492(2002).
[12]
INVOLVEMENT IN SCZD, AND VARIANT VAL-222.
PubMed=15729744; DOI=10.1002/ajmg.b.30170;
Lewis S.J., Zammit S., Gunnell D., Smith G.D.;
"A meta-analysis of the MTHFR C677T polymorphism and schizophrenia
risk.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 135B:2-4(2005).
[13]
INVOLVEMENT IN SCZD, AND VARIANT VAL-222.
PubMed=18583979; DOI=10.1038/ng.171;
Allen N.C., Bagade S., McQueen M.B., Ioannidis J.P., Kavvoura F.K.,
Khoury M.J., Tanzi R.E., Bertram L.;
"Systematic meta-analyses and field synopsis of genetic association
studies in schizophrenia: the SzGene database.";
Nat. Genet. 40:827-834(2008).
[14]
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).
[15]
VARIANTS MTHFRD GLN-52; MET-227; LEU-251; CYS-325; CYS-335 AND
CYS-357, AND SEQUENCE REVISION TO 177.
PubMed=7726158;
Goyette P., Frosst P., Rosenblatt D.S., Rozen R.;
"Seven novel mutations in the methylenetetrahydrofolate reductase gene
and genotype/phenotype correlations in severe
methylenetetrahydrofolate reductase deficiency.";
Am. J. Hum. Genet. 56:1052-1059(1995).
[16]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT VAL-222.
PubMed=7564788; DOI=10.1016/S0140-6736(95)91743-8;
van der Put N.M.J., Steegers-Theunissen R.P.M., Frosst P.,
Trijbels F.J.M., Eskes T.K.A.B., van den Heuvel L.P., Mariman E.C.M.,
den Heyer M., Rozen R., Blom H.J.;
"Mutated methylenetetrahydrofolate reductase as a risk factor for
spina bifida.";
Lancet 346:1070-1071(1995).
[17]
VARIANT VAL-222.
PubMed=7647779; DOI=10.1038/ng0595-111;
Frosst P., Blom H.J., Milos R., Goyette P., Sheppard C.A.,
Matthews R.G., Boers G.J.H., den Heijer M., Kluijtmans L.A.J.,
van den Heuvel L.P., Rozen R.;
"A candidate genetic risk factor for vascular disease: a common
mutation in methylenetetrahydrofolate reductase.";
Nat. Genet. 10:111-113(1995).
[18]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT VAL-222.
PubMed=8826441;
DOI=10.1002/(SICI)1096-8628(19960628)63:4<610::AID-AJMG15>3.0.CO;2-L;
Ou C.Y., Stevenson R.E., Brown V.K., Schwartz C.E., Allen W.P.,
Khoury M.J., Rozen R., Oakley G.P. Jr., Adams M.J. Jr.;
"5,10 Methylenetetrahydrofolate reductase genetic polymorphism as a
risk factor for neural tube defects.";
Am. J. Med. Genet. 63:610-614(1996).
[19]
VARIANTS MTHFRD PRO-51; PRO-323 AND CYS-377.
PubMed=8940272;
Goyette P., Christensen B., Rosenblatt D.S., Rozen R.;
"Severe and mild mutations in cis for the methylenetetrahydrofolate
reductase (MTHFR) gene, and description of five novel mutations in
MTHFR.";
Am. J. Hum. Genet. 59:1268-1275(1996).
[20]
INVERSE ASSOCIATION OF VARIANT VAL-222 WITH COLORECTAL CANCER.
PubMed=8895734;
Chen J., Giovannucci E., Kelsey K., Rimm E.B., Stampfer M.J.,
Colditz G.A., Spiegelman D., Willett W.C., Hunter D.J.;
"A methylenetetrahydrofolate reductase polymorphism and the risk of
colorectal cancer.";
Cancer Res. 56:4862-4864(1996).
[21]
VARIANT VAL-222.
PubMed=9545406; DOI=10.1086/301836;
Schneider J.A., Rees D.C., Liu Y.-T., Clegg J.B.;
"Worldwide distribution of a common methylenetetrahydrofolate
reductase mutation.";
Am. J. Hum. Genet. 62:1258-1260(1998).
[22]
VARIANT ALA-429.
PubMed=9545395; DOI=10.1086/301825;
van der Put N.M.J., Gabreels F., Stevens E.M.B., Smeitink J.A.M.,
Trijbels F.J.M., Eskes T.K.A.B., van den Heuvel L.P., Blom H.J.;
"A second mutation in the methylenetetrahydrofolate reductase gene: an
additional risk factor for neural-tube defects?";
Am. J. Hum. Genet. 62:1044-1051(1998).
[23]
VARIANTS MTHFRD SER-324 AND GLY-339.
PubMed=9781030; DOI=10.1038/sj.ejhg.5200182;
Kluijtmans L.A.J., Wendel U., Stevens E.M.B., van den Heuvel L.P.W.J.,
Trijbels F.J.M., Blom H.J.;
"Identification of four novel mutations in severe
methylenetetrahydrofolate reductase deficiency.";
Eur. J. Hum. Genet. 6:257-265(1998).
[24]
VARIANT ALA-429.
PubMed=9719624; DOI=10.1006/mgme.1998.2714;
Weisberg I., Tran P., Christiensen B., Sibani S., Rozen R.;
"A second genetic polymorphism in methylenetetrahydrofolate reductase
(MTHFR) associated with decreased enzyme activity.";
Mol. Genet. Metab. 64:169-172(1998).
[25]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT VAL-222.
PubMed=10323741;
DOI=10.1002/(SICI)1096-8628(19990521)84:2<151::AID-AJMG12>3.0.CO;2-T;
Christensen B., Arbour L., Tran P., Leclerc D., Sabbaghian N.,
Platt R., Gilfix B.M., Rosenblatt D.S., Gravel R.A., Forbes P.,
Rozen R.;
"Genetic polymorphisms in methylenetetrahydrofolate reductase and
methionine synthase, folate levels in red blood cells, and risk of
neural tube defects.";
Am. J. Med. Genet. 84:151-157(1999).
[26]
VARIANTS VAL-222 AND ALA-429, AND ASSOCIATION WITH SUSCEPTIBILITY TO
ACUTE LEUKEMIA.
PubMed=10536004; DOI=10.1073/pnas.96.22.12810;
Skibola C.F., Smith M.T., Kane E., Roman E., Rollinson S.,
Cartwright R.A., Morgan G.;
"Polymorphisms in the methylenetetrahydrofolate reductase gene are
associated with susceptibility to acute leukemia in adults.";
Proc. Natl. Acad. Sci. U.S.A. 96:12810-12815(1999).
[27]
VARIANTS MTHFRD ASP-387; LEU-572 AND LYS-586.
PubMed=10679944;
DOI=10.1002/(SICI)1098-1004(200003)15:3<280::AID-HUMU9>3.0.CO;2-I;
Sibani S., Christensen B., O'Ferrall E., Saadi I., Hiou-Tim F.,
Rosenblatt D.S., Rozen R.;
"Characterization of six novel mutations in the
methylenetetrahydrofolate reductase (MTHFR) gene in patients with
homocystinuria.";
Hum. Mutat. 15:280-287(2000).
[28]
ASSOCIATION OF VARIANT VAL-222 WITH SUSCEPTIBILITY TO ISCHSTR.
PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[29]
VARIANT [LARGE SCALE ANALYSIS] ALA-470.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[30]
VARIANTS MTHFRD LEU-218; SER-435 AND GLY-574, CHARACTERIZATION OF
VARIANT MTHFRD LEU-218, CHARACTERIZATION OF VARIANT VAL-222, AND
COFACTOR.
PubMed=20236116; DOI=10.1111/j.1399-0004.2010.01391.x;
Urreizti R., Moya-Garcia A.A., Pino-Angeles A., Cozar M.,
Langkilde A., Fanhoe U., Esteves C., Arribas J., Vilaseca M.A.,
Perez-Duenas B., Pineda M., Gonzalez V., Artuch R., Baldellou A.,
Vilarinho L., Fowler B., Ribes A., Sanchez-Jimenez F., Grinberg D.,
Balcells S.;
"Molecular characterization of five patients with homocystinuria due
to severe methylenetetrahydrofolate reductase deficiency.";
Clin. Genet. 78:441-448(2010).
[31]
VARIANT MTHFRD SER-435.
PubMed=25818041; DOI=10.1111/epi.12954;
Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A.,
Moharir M., Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
"Diagnostic yield of genetic testing in epileptic encephalopathy in
childhood.";
Epilepsia 56:707-716(2015).
[32]
VARIANTS MTHFRD GLN-46; TRP-46; GLN-52; SER-59; GLY-68; TRP-82;
THR-113; TYR-127; ASN-129; ARG-130; PRO-147; VAL-149; MET-153;
GLN-157; THR-175; GLN-183; VAL-195; ASP-196; LYS-215 DEL; LEU-225;
ILE-226 DEL; PHE-253; SER-254; VAL-255; ASN-256; VAL-257; HIS-335;
THR-338; GLY-339; SER-348; TYR-354; HIS-363; GLU-372; CYS-377;
HIS-377; ASP-387; SER-421; ASP-506; PHE-536; LEU-572; GLY-574;
GLY-575; PRO-598 AND PRO-628, CHARACTERIZATION OF VARIANTS MTHFRD
GLN-46; TRP-46; GLN-52; SER-59; GLY-68; TRP-82; THR-113; TYR-127;
ASN-129; ARG-130; PRO-147; VAL-149; MET-153; GLN-157; THR-175;
GLN-183; VAL-195; ASP-196; LYS-215 DEL; LEU-225; ILE-226 DEL; PHE-253;
SER-254; VAL-255; ASN-256; VAL-257; HIS-335; THR-338; GLY-339;
SER-348; TYR-354; HIS-363; GLU-372; CYS-377; HIS-377; ASP-387;
SER-421; ASP-506; PHE-536; LEU-572; GLY-574; GLY-575; PRO-598 AND
PRO-628, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=25736335; DOI=10.1002/humu.22779;
Burda P., Schaefer A., Suormala T., Rummel T., Buerer C.,
Heuberger D., Frapolli M., Giunta C., Sokolova J., Vlaskova H.,
Kozich V., Koch H.G., Fowler B., Froese D.S., Baumgartner M.R.;
"Insights into severe 5,10-methylenetetrahydrofolate reductase
deficiency: molecular genetic and enzymatic characterization of 76
patients.";
Hum. Mutat. 36:611-621(2015).
-!- FUNCTION: Catalyzes the conversion of 5,10-
methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-
substrate for homocysteine remethylation to methionine.
{ECO:0000269|PubMed:25736335}.
-!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10-
methylenetetrahydrofolate + NAD(P)H.
{ECO:0000269|PubMed:25736335}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:20236116};
-!- ENZYME REGULATION: Allosterically regulated by S-
adenosylmethionine.
-!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
-!- SUBUNIT: Homodimer.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P42898-1; Sequence=Displayed;
Name=2;
IsoId=P42898-2; Sequence=VSP_053744;
-!- POLYMORPHISM: Genetic variation in MTHFR influences susceptibility
to occlusive vascular disease, neural tube defects (NTD), colon
cancer and acute leukemia.
-!- DISEASE: Methylenetetrahydrofolate reductase deficiency (MTHFRD)
[MIM:236250]: Autosomal recessive disorder with a wide range of
features including homocysteinuria, homocysteinemia [MIM:603174],
developmental delay, severe mental retardation, perinatal death,
psychiatric disturbances, and later-onset neurodegenerative
disorders. {ECO:0000269|PubMed:10679944,
ECO:0000269|PubMed:20236116, ECO:0000269|PubMed:25736335,
ECO:0000269|PubMed:25818041, ECO:0000269|PubMed:7726158,
ECO:0000269|PubMed:8940272, ECO:0000269|PubMed:9781030}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
acute neurologic event leading to death of neural tissue of the
brain and resulting in loss of motor, sensory and/or cognitive
function. Ischemic strokes, resulting from vascular occlusion, is
considered to be a highly complex disease consisting of a group of
heterogeneous disorders with multiple genetic and environmental
risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease
susceptibility is associated with variations 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:10323741,
ECO:0000269|PubMed:7564788, ECO:0000269|PubMed:8826441}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex,
multifactorial psychotic disorder or group of disorders
characterized by disturbances in the form and content of thought
(e.g. delusions, hallucinations), in mood (e.g. inappropriate
affect), in sense of self and relationship to the external world
(e.g. loss of ego boundaries, withdrawal), and in behavior (e.g
bizarre or apparently purposeless behavior). Although it affects
emotions, it is distinguished from mood disorders in which such
disturbances are primary. Similarly, there may be mild impairment
of cognitive function, and it is distinguished from the dementias
in which disturbed cognitive function is considered primary. Some
patients manifest schizophrenic as well as bipolar disorder
symptoms and are often given the diagnosis of schizoaffective
disorder. {ECO:0000269|PubMed:15729744,
ECO:0000269|PubMed:18583979}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MTHFRID41448ch1p36.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mthfr/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=MTHFR";
-!- WEB RESOURCE: Name=Wikipedia; Note=Methylenetetrahydrofolate
reductase entry;
URL="https://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase";
-----------------------------------------------------------------------
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EMBL; U09806; AAA74440.2; -; mRNA.
EMBL; AF105987; AAD17965.1; -; Genomic_DNA.
EMBL; AF105977; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105978; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105979; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105980; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105981; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105982; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105983; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105984; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105985; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AF105986; AAD17965.1; JOINED; Genomic_DNA.
EMBL; AJ237672; CAB41971.1; -; mRNA.
EMBL; AK312907; BAG35753.1; -; mRNA.
EMBL; AY338232; AAP88033.1; -; Genomic_DNA.
EMBL; AL953897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471130; EAW71709.1; -; Genomic_DNA.
EMBL; BC053509; AAH53509.1; -; mRNA.
EMBL; AY046562; AAL17648.1; -; mRNA.
EMBL; AF398930; AAN40865.1; -; Genomic_DNA.
CCDS; CCDS137.1; -. [P42898-1]
CCDS; CCDS81262.1; -. [P42898-2]
PIR; S46454; S46454.
RefSeq; NP_001317287.1; NM_001330358.1. [P42898-2]
RefSeq; NP_005948.3; NM_005957.4. [P42898-1]
RefSeq; XP_005263517.1; XM_005263460.4. [P42898-1]
RefSeq; XP_005263519.1; XM_005263462.4. [P42898-1]
UniGene; Hs.214142; -.
UniGene; Hs.737916; -.
PDB; 6FCX; X-ray; 2.50 A; A/B=37-644.
PDBsum; 6FCX; -.
ProteinModelPortal; P42898; -.
SMR; P42898; -.
BioGrid; 110624; 26.
IntAct; P42898; 2.
MINT; P42898; -.
STRING; 9606.ENSP00000365775; -.
DrugBank; DB00542; Benazepril.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00158; Folic Acid.
DrugBank; DB00134; L-Methionine.
DrugBank; DB00170; Menadione.
DrugBank; DB00563; Methotrexate.
DrugBank; DB00140; Riboflavin.
DrugBank; DB00116; Tetrahydrofolic acid.
iPTMnet; P42898; -.
PhosphoSitePlus; P42898; -.
BioMuta; MTHFR; -.
DMDM; 56405339; -.
EPD; P42898; -.
MaxQB; P42898; -.
PaxDb; P42898; -.
PeptideAtlas; P42898; -.
PRIDE; P42898; -.
ProteomicsDB; 55566; -.
Ensembl; ENST00000376583; ENSP00000365767; ENSG00000177000. [P42898-2]
Ensembl; ENST00000376585; ENSP00000365770; ENSG00000177000. [P42898-2]
Ensembl; ENST00000376590; ENSP00000365775; ENSG00000177000. [P42898-1]
Ensembl; ENST00000376592; ENSP00000365777; ENSG00000177000. [P42898-1]
GeneID; 4524; -.
KEGG; hsa:4524; -.
UCSC; uc001atc.3; human. [P42898-1]
CTD; 4524; -.
DisGeNET; 4524; -.
EuPathDB; HostDB:ENSG00000177000.10; -.
GeneCards; MTHFR; -.
HGNC; HGNC:7436; MTHFR.
HPA; HPA063389; -.
MalaCards; MTHFR; -.
MIM; 181500; phenotype.
MIM; 236250; phenotype.
MIM; 601367; phenotype.
MIM; 601634; phenotype.
MIM; 603174; phenotype.
MIM; 607093; gene.
neXtProt; NX_P42898; -.
OpenTargets; ENSG00000177000; -.
Orphanet; 268392; Cervical spina bifida aperta.
Orphanet; 268762; Cervical spina bifida cystica.
Orphanet; 268397; Cervicothoracic spina bifida aperta.
Orphanet; 268766; Cervicothoracic spina bifida cystica.
Orphanet; 395; Homocystinuria due to methylene tetrahydrofolate reductase deficiency.
Orphanet; 1048; Isolated anencephaly/exencephaly.
Orphanet; 268388; Lumbosacral spina bifida aperta.
Orphanet; 268758; Lumbosacral spina bifida cystica.
Orphanet; 413690; Methotrexate toxicity or dose selection.
Orphanet; 64738; Non rare thrombophilia.
Orphanet; 268384; Thoracolumbosacral spina bifida aperta.
Orphanet; 268752; Thoracolumbosacral spina bifida cystica.
Orphanet; 268377; Total spina bifida aperta.
Orphanet; 268748; Total spina bifida cystica.
Orphanet; 268740; Upper thoracic spina bifida aperta.
Orphanet; 268770; Upper thoracic spina bifida cystica.
PharmGKB; PA245; -.
eggNOG; KOG0564; Eukaryota.
eggNOG; COG0685; LUCA.
GeneTree; ENSGT00390000012490; -.
HOGENOM; HOG000246234; -.
HOVERGEN; HBG006414; -.
InParanoid; P42898; -.
KO; K00297; -.
OMA; MESGDKW; -.
OrthoDB; EOG091G0YQK; -.
PhylomeDB; P42898; -.
TreeFam; TF105665; -.
BRENDA; 1.5.1.20; 2681.
Reactome; R-HSA-196757; Metabolism of folate and pterines.
SABIO-RK; P42898; -.
SIGNOR; P42898; -.
UniPathway; UPA00193; -.
ChiTaRS; MTHFR; human.
GeneWiki; Methylenetetrahydrofolate_reductase; -.
GenomeRNAi; 4524; -.
PRO; PR:P42898; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000177000; -.
CleanEx; HS_MTHFR; -.
ExpressionAtlas; P42898; baseline and differential.
Genevisible; P42898; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:BHF-UCL.
GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IDA:BHF-UCL.
GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
GO; GO:0050661; F:NADP binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0046655; P:folic acid metabolic process; TAS:Reactome.
GO; GO:0070829; P:heterochromatin maintenance; IDA:BHF-UCL.
GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
GO; GO:0006555; P:methionine metabolic process; IGI:BHF-UCL.
GO; GO:0031060; P:regulation of histone methylation; IDA:BHF-UCL.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0033274; P:response to vitamin B2; IEA:Ensembl.
GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl.
GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL.
CDD; cd00537; MTHFR; 1.
InterPro; IPR029041; FAD-linked_oxidoreductase-like.
InterPro; IPR004621; Fadh2_euk.
InterPro; IPR003171; Mehydrof_redctse.
Pfam; PF02219; MTHFR; 1.
SUPFAM; SSF51730; SSF51730; 1.
TIGRFAMs; TIGR00677; fadh2_euk; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing;
Complete proteome; Disease mutation; FAD; Flavoprotein; NADP;
Oxidoreductase; Polymorphism; Reference proteome; Schizophrenia.
CHAIN 1 656 Methylenetetrahydrofolate reductase.
/FTId=PRO_0000190245.
NP_BIND 63 68 NAD. {ECO:0000250}.
NP_BIND 94 95 NAD and FAD. {ECO:0000250}.
NP_BIND 157 159 FAD. {ECO:0000250}.
NP_BIND 174 175 FAD. {ECO:0000250}.
NP_BIND 201 204 FAD. {ECO:0000250}.
ACT_SITE 63 63 Proton donor/acceptor. {ECO:0000250}.
BINDING 127 127 FAD. {ECO:0000250}.
BINDING 159 159 Substrate. {ECO:0000250}.
BINDING 197 197 FAD. {ECO:0000250}.
BINDING 210 210 FAD. {ECO:0000250}.
BINDING 217 217 FAD. {ECO:0000250}.
BINDING 228 228 Substrate. {ECO:0000250}.
BINDING 321 321 Substrate. {ECO:0000250}.
BINDING 325 325 Substrate. {ECO:0000250}.
VAR_SEQ 1 1 M -> MDHRKARVLPAGHYCPSLGIWASQVGSVRSSVPPSI
SRNPAM (in isoform 2).
{ECO:0000303|PubMed:12370778}.
/FTId=VSP_053744.
VARIANT 46 46 R -> Q (in MTHFRD; reduces
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs776483190).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074111.
VARIANT 46 46 R -> W (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs138189536).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074112.
VARIANT 51 51 R -> P (in MTHFRD; dbSNP:rs201618781).
{ECO:0000269|PubMed:8940272}.
/FTId=VAR_009530.
VARIANT 52 52 R -> Q (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs754980119).
{ECO:0000269|PubMed:25736335,
ECO:0000269|PubMed:7726158}.
/FTId=VAR_004319.
VARIANT 59 59 W -> S (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs786204007).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074113.
VARIANT 68 68 R -> G (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs763539350).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074114.
VARIANT 68 68 R -> Q (in dbSNP:rs2066472).
{ECO:0000269|Ref.5}.
/FTId=VAR_014881.
VARIANT 82 82 R -> W (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs786204009).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074115.
VARIANT 113 113 A -> T (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs147257424).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074116.
VARIANT 127 127 H -> Y (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs769381688).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074117.
VARIANT 129 129 T -> N (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074118.
VARIANT 130 130 C -> R (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs786204012).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074119.
VARIANT 147 147 Q -> P (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs786204013).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074120.
VARIANT 149 149 G -> V (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity). {ECO:0000269|PubMed:25736335}.
/FTId=VAR_074121.
VARIANT 153 153 I -> M (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs767890671).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074122.
VARIANT 157 157 R -> Q (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs121434295).
{ECO:0000269|PubMed:25736335,
ECO:0000269|PubMed:7920641}.
/FTId=VAR_004320.
VARIANT 175 175 A -> T (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074123.
VARIANT 183 183 R -> Q (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs574132670).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074124.
VARIANT 195 195 A -> V (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs760161369).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074125.
VARIANT 196 196 G -> D (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204014).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074126.
VARIANT 215 215 Missing (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity). {ECO:0000269|PubMed:25736335}.
/FTId=VAR_074127.
VARIANT 218 218 V -> L (in MTHFRD; decreased affinity for
FAD cofactor).
{ECO:0000269|PubMed:20236116}.
/FTId=VAR_074128.
VARIANT 222 222 A -> V (common polymorphism; at
homozygosity reduces the risk for
colorectal cancer in individuals with
adequate folate status; decreased risk
for adult acute leukemia; increased risk
for NTDFS; increased risk for
schizophrenia; thermolabile; decreased
affinity for FAD cofactor; 50% reduced
activity; dbSNP:rs1801133).
{ECO:0000269|PubMed:10536004,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15729744,
ECO:0000269|PubMed:18583979,
ECO:0000269|PubMed:20236116,
ECO:0000269|PubMed:7647779,
ECO:0000269|PubMed:9545406,
ECO:0000269|Ref.5}.
/FTId=VAR_009528.
VARIANT 225 225 I -> L (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs200100285).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074129.
VARIANT 226 226 Missing (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074130.
VARIANT 227 227 T -> M (in MTHFRD; dbSNP:rs748571395).
{ECO:0000269|PubMed:7726158}.
/FTId=VAR_004321.
VARIANT 251 251 P -> L (in MTHFRD).
{ECO:0000269|PubMed:7726158}.
/FTId=VAR_004322.
VARIANT 253 253 V -> F (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074131.
VARIANT 254 254 P -> S (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs786204017).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074132.
VARIANT 255 255 G -> V (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs786204018).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074133.
VARIANT 256 256 I -> N (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs373398993).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074134.
VARIANT 257 257 F -> V (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs786204019).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074135.
VARIANT 323 323 L -> P (in MTHFRD; dbSNP:rs121434297).
{ECO:0000269|PubMed:8940272}.
/FTId=VAR_009531.
VARIANT 324 324 N -> S (in MTHFRD; dbSNP:rs267606887).
{ECO:0000269|PubMed:9781030}.
/FTId=VAR_009532.
VARIANT 325 325 R -> C (in MTHFRD; dbSNP:rs371085894).
{ECO:0000269|PubMed:7726158}.
/FTId=VAR_004323.
VARIANT 335 335 R -> C (in MTHFRD; dbSNP:rs748289202).
{ECO:0000269|PubMed:7726158}.
/FTId=VAR_004324.
VARIANT 335 335 R -> H (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; no effect on affinity for
NADPH; dbSNP:rs543016186).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074136.
VARIANT 338 338 M -> T (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs368321176).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074137.
VARIANT 339 339 W -> G (in MTHFRD; loss of
methylenetetrahydrofolate reductase
activity; dbSNP:rs267606886).
{ECO:0000269|PubMed:25736335,
ECO:0000269|PubMed:9781030}.
/FTId=VAR_009533.
VARIANT 348 348 P -> S (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204021).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074138.
VARIANT 354 354 H -> Y (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204022).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074139.
VARIANT 357 357 R -> C (in MTHFRD; dbSNP:rs779993607).
{ECO:0000269|PubMed:7726158}.
/FTId=VAR_004325.
VARIANT 363 363 R -> H (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204023).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074140.
VARIANT 372 372 K -> E (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204024).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074141.
VARIANT 377 377 R -> C (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs121434296).
{ECO:0000269|PubMed:25736335,
ECO:0000269|PubMed:8940272}.
/FTId=VAR_009534.
VARIANT 377 377 R -> H (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs750323424).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074142.
VARIANT 387 387 G -> D (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:10679944,
ECO:0000269|PubMed:25736335}.
/FTId=VAR_009535.
VARIANT 421 421 W -> S (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs200137991).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074143.
VARIANT 422 422 G -> R (in dbSNP:rs45571736).
{ECO:0000269|Ref.5}.
/FTId=VAR_018857.
VARIANT 429 429 E -> A (common polymorphism; decreased
risk for adult acute leukemia;
thermolabile; decreased activity;
dbSNP:rs1801131).
{ECO:0000269|PubMed:10536004,
ECO:0000269|PubMed:9545395,
ECO:0000269|PubMed:9719624,
ECO:0000269|Ref.5}.
/FTId=VAR_014882.
VARIANT 435 435 F -> S (in MTHFRD; dbSNP:rs754015864).
{ECO:0000269|PubMed:20236116,
ECO:0000269|PubMed:25818041}.
/FTId=VAR_074144.
VARIANT 470 470 E -> A. {ECO:0000269|PubMed:18987736}.
/FTId=VAR_054158.
VARIANT 506 506 Y -> D (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204026).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074145.
VARIANT 519 519 R -> C (in dbSNP:rs45496998).
{ECO:0000269|Ref.5}.
/FTId=VAR_018858.
VARIANT 519 519 R -> H (in dbSNP:rs45449298).
/FTId=VAR_050293.
VARIANT 536 536 V -> F (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204028).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074146.
VARIANT 566 566 G -> E (in dbSNP:rs2274974).
/FTId=VAR_050294.
VARIANT 572 572 P -> L (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs144508139).
{ECO:0000269|PubMed:10679944,
ECO:0000269|PubMed:25736335}.
/FTId=VAR_009536.
VARIANT 574 574 V -> G (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH).
{ECO:0000269|PubMed:20236116,
ECO:0000269|PubMed:25736335}.
/FTId=VAR_074147.
VARIANT 575 575 V -> G (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204031).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074148.
VARIANT 586 586 E -> K (in MTHFRD; dbSNP:rs983672500).
{ECO:0000269|PubMed:10679944}.
/FTId=VAR_009537.
VARIANT 594 594 R -> Q (in dbSNP:rs2274976).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_018859.
VARIANT 598 598 L -> P (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204034).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074149.
VARIANT 628 628 L -> P (in MTHFRD; reduced
methylenetetrahydrofolate reductase
activity; reduced affinity for NADPH;
dbSNP:rs786204037).
{ECO:0000269|PubMed:25736335}.
/FTId=VAR_074150.
VARIANT 653 653 T -> M (in dbSNP:rs35737219).
{ECO:0000269|Ref.5}.
/FTId=VAR_018860.
SEQUENCE 656 AA; 74597 MW; F16E774833D054B8 CRC64;
MVNEARGNSS LNPCLEGSAS SGSESSKDSS RCSTPGLDPE RHERLREKMR RRLESGDKWF
SLEFFPPRTA EGAVNLISRF DRMAAGGPLY IDVTWHPAGD PGSDKETSSM MIASTAVNYC
GLETILHMTC CRQRLEEITG HLHKAKQLGL KNIMALRGDP IGDQWEEEEG GFNYAVDLVK
HIRSEFGDYF DICVAGYPKG HPEAGSFEAD LKHLKEKVSA GADFIITQLF FEADTFFRFV
KACTDMGITC PIVPGIFPIQ GYHSLRQLVK LSKLEVPQEI KDVIEPIKDN DAAIRNYGIE
LAVSLCQELL ASGLVPGLHF YTLNREMATT EVLKRLGMWT EDPRRPLPWA LSAHPKRREE
DVRPIFWASR PKSYIYRTQE WDEFPNGRWG NSSSPAFGEL KDYYLFYLKS KSPKEELLKM
WGEELTSEES VFEVFVLYLS GEPNRNGHKV TCLPWNDEPL AAETSLLKEE LLRVNRQGIL
TINSQPNING KPSSDPIVGW GPSGGYVFQK AYLEFFTSRE TAEALLQVLK KYELRVNYHL
VNVKGENITN APELQPNAVT WGIFPGREII QPTVVDPVSF MFWKDEAFAL WIERWGKLYE
EESPSRTIIQ YIHDNYFLVN LVDNDFPLDN CLWQVVEDTL ELLNRPTQNA RETEAP


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