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Dihydrofolate reductase (EC 1.5.1.3)

 DYR_HUMAN               Reviewed;         187 AA.
P00374; B4DDD2; Q14130; Q6IRW8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 195.
RecName: Full=Dihydrofolate reductase;
EC=1.5.1.3;
Name=DHFR;
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].
PubMed=6323448;
Chen M.-J., Shimada T., Moulton A.D., Cline A., Humphries R.K.,
Maizel J., Nienhuis A.W.;
"The functional human dihydrofolate reductase gene.";
J. Biol. Chem. 259:3933-3943(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=6687716; DOI=10.1016/0378-1119(83)90147-6;
Masters J.N., Attardi G.;
"The nucleotide sequence of the cDNA coding for the human dihydrofolic
acid reductase.";
Gene 21:59-63(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6235374; DOI=10.1016/0022-2836(84)90419-4;
Yang J.K., Masters J.N., Attardi G.;
"Human dihydrofolate reductase gene organization. Extensive
conservation of the G + C-rich 5' non-coding sequence and strong
intron size divergence from homologous mammalian genes.";
J. Mol. Biol. 176:169-187(1984).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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]
TISSUE SPECIFICITY, AND VARIANT DHFRD PHE-80.
PubMed=21310276; DOI=10.1016/j.ajhg.2011.01.004;
Banka S., Blom H.J., Walter J., Aziz M., Urquhart J., Clouthier C.M.,
Rice G.I., de Brouwer A.P., Hilton E., Vassallo G., Will A.,
Smith D.E., Smulders Y.M., Wevers R.A., Steinfeld R., Heales S.,
Crow Y.J., Pelletier J.N., Jones S., Newman W.G.;
"Identification and characterization of an inborn error of metabolism
caused by dihydrofolate reductase deficiency.";
Am. J. Hum. Genet. 88:216-225(2011).
[8]
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).
[9]
CATALYTIC ACTIVITY, RNA-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21876184; DOI=10.1073/pnas.1103605108;
McEntee G., Minguzzi S., O'Brien K., Ben Larbi N., Loscher C.,
O'Fagain C., Parle-McDermott A.;
"The former annotated human pseudogene dihydrofolate reductase-like 1
(DHFRL1) is expressed and functional.";
Proc. Natl. Acad. Sci. U.S.A. 108:15157-15162(2011).
[10]
FUNCTION.
PubMed=21876188; DOI=10.1073/pnas.1103623108;
Anderson D.D., Quintero C.M., Stover P.J.;
"Identification of a de novo thymidylate biosynthesis pathway in
mammalian mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FOLATE.
PubMed=3383852; DOI=10.1111/j.1432-1033.1988.tb14108.x;
Oefner C., D'Arcy A., Winkler F.K.;
"Crystal structure of human dihydrofolate reductase complexed with
folate.";
Eur. J. Biochem. 174:377-385(1988).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH FOLATE AND
5-DEAZAFOLATE, AND SUBUNIT.
PubMed=2248959; DOI=10.1021/bi00492a021;
Davies J.F., Delcamp T.J., Prendergast N.J., Ashford V.A.,
Freisheim J.H., Kraut J.;
"Crystal structures of recombinant human dihydrofolate reductase
complexed with folate and 5-deazafolate.";
Biochemistry 29:9467-9479(1990).
[13]
STRUCTURE BY NMR.
PubMed=1731871; DOI=10.1021/bi00116a031;
Stockman B.J., Nirmala N.R., Wagner G., Delcamp T.J., Deyarman M.T.,
Freisheim J.H.;
"Sequence-specific 1H and 15N resonance assignments for human
dihydrofolate reductase in solution.";
Biochemistry 31:218-229(1992).
[14]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH NADPH;
PIRITREXIM AND METOTHREXATE, AND MUTAGENESIS OF LEU-23.
PubMed=7890613; DOI=10.1074/jbc.270.10.5057;
Lewis W.S., Cody V., Galitsky N., Luft J.R., Pangborn W.,
Chunduru S.K., Spencer H.T., Appleman J.R., Blakley R.L.;
"Methotrexate-resistant variants of human dihydrofolate reductase with
substitutions of leucine 22. Kinetics, crystallography, and potential
as selectable markers.";
J. Biol. Chem. 270:5057-5064(1995).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=9374868; DOI=10.1021/bi971711l;
Cody V., Galitsky N., Luft J.R., Pangborn W., Blakley R.L.,
Gangjee A.;
"Comparison of two independent crystal structures of human
dihydrofolate reductase ternary complexes reduced with nicotinamide
adenine dinucleotide phosphate and the very tight-binding inhibitor
PT523.";
Biochemistry 36:13897-13903(1997).
[16]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH NADPH AND
QUINAZOLINE INHIBITORS, AND CATALYTIC ACTIVITY.
PubMed=9719595; DOI=10.1021/jm980081y;
Gangjee A., Vidwans A.P., Vasudevan A., Queener S.F., Kisliuk R.L.,
Cody V., Li R., Galitsky N., Luft J.R., Pangborn W.;
"Structure-based design and synthesis of lipophilic 2,4-diamino-6-
substituted quinazolines and their evaluation as inhibitors of
dihydrofolate reductases and potential antitumor agents.";
J. Med. Chem. 41:3426-3434(1998).
[17]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEXES WITH NADP AND THE
SYNTHETIC INHIBITORS SRI-9439 AND SRI-9662, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=12096917; DOI=10.1016/S0022-2836(02)00469-2;
Klon A.E., Heroux A., Ross L.J., Pathak V., Johnson C.A., Piper J.R.,
Borhani D.W.;
"Atomic structures of human dihydrofolate reductase complexed with
NADPH and two lipophilic antifolates at 1.09 A and 1.05 A
resolution.";
J. Mol. Biol. 320:677-693(2002).
[18]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=12657784; DOI=10.1107/S0907444903001951;
Cody V., Galitsky N., Luft J.R., Pangborn W., Gangjee A.;
"Analysis of two polymorphic forms of a pyrido[2,3-d]pyrimidine N9-C10
reversed-bridge antifolate binary complex with human dihydrofolate
reductase.";
Acta Crystallogr. D 59:654-661(2003).
[19]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=12925791; DOI=10.1107/S0907444903014963;
Cody V., Luft J.R., Pangborn W., Gangjee A.;
"Analysis of three crystal structure determinations of a 5-methyl-6-N-
methylanilino pyridopyrimidine antifolate complex with human
dihydrofolate reductase.";
Acta Crystallogr. D 59:1603-1609(2003).
[20]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADPH AND
INHIBITOR, MUTAGENESIS OF GLN-36 AND ASN-65, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15039552; DOI=10.1107/S0907444904002094;
Cody V., Luft J.R., Pangborn W., Gangjee A., Queener S.F.;
"Structure determination of tetrahydroquinazoline antifolates in
complex with human and Pneumocystis carinii dihydrofolate reductase:
correlations between enzyme selectivity and stereochemistry.";
Acta Crystallogr. D 60:646-655(2004).
[21]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEXES WITH NADP AND
METHOTREXATE, AND MUTAGENESIS OF LEU-23.
PubMed=15681865; DOI=10.1107/S0907444904030422;
Cody V., Luft J.R., Pangborn W.;
"Understanding the role of Leu22 variants in methotrexate resistance:
comparison of wild-type and Leu22Arg variant mouse and human
dihydrofolate reductase ternary crystal complexes with methotrexate
and NADPH.";
Acta Crystallogr. D 61:147-155(2005).
[22]
STRUCTURE BY NMR IN COMPLEX WITH TRIMETHOPRIM AND NADPH.
PubMed=16222560; DOI=10.1007/s10858-005-1475-z;
Kovalevskaya N.V., Smurnyy Y.D., Polshakov V.I., Birdsall B.,
Bradbury A.F., Frenkiel T., Feeney J.;
"Solution structure of human dihydrofolate reductase in its complex
with trimethoprim and NADPH.";
J. Biomol. NMR 33:69-72(2005).
[23]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEXES WITH NADP AND
BORON-CONTAINING INHIBITORS, AND CATALYTIC ACTIVITY.
PubMed=17569517; DOI=10.1021/jm0701977;
Reynolds R.C., Campbell S.R., Fairchild R.G., Kisliuk R.L.,
Micca P.L., Queener S.F., Riordan J.M., Sedwick W.D., Waud W.R.,
Leung A.K., Dixon R.W., Suling W.J., Borhani D.W.;
"Novel boron-containing, nonclassical antifolates: synthesis and
preliminary biological and structural evaluation.";
J. Med. Chem. 50:3283-3289(2007).
[24]
X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEXES WITH NADP AND THE
SYNTHETIC INHIBITOR PY957, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF GLN-36 AND ASN-65.
PubMed=19196009; DOI=10.1021/bi801960h;
Cody V., Pace J., Makin J., Piraino J., Queener S.F., Rosowsky A.;
"Correlations of inhibitor kinetics for Pneumocystis jirovecii and
human dihydrofolate reductase with structural data for human active
site mutant enzyme complexes.";
Biochemistry 48:1702-1711(2009).
[25]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ARG-32/GLU-36 IN
COMPLEX WITH METHOTREXATE AND NADP, MUTAGENESIS OF PHE-32 AND GLN-36,
AND CATALYTIC ACTIVITY.
PubMed=19478082; DOI=10.1074/jbc.M109.018010;
Volpato J.P., Yachnin B.J., Blanchet J., Guerrero V., Poulin L.,
Fossati E., Berghuis A.M., Pelletier J.N.;
"Multiple conformers in active site of human dihydrofolate reductase
F31R/Q35E double mutant suggest structural basis for methotrexate
resistance.";
J. Biol. Chem. 284:20079-20089(2009).
[26]
X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 1-187.
PubMed=19719239; DOI=10.1021/jm900490a;
Gangjee A., Li W., Kisliuk R.L., Cody V., Pace J., Piraino J.,
Makin J.;
"Design, synthesis, and X-ray crystal structure of classical and
nonclassical 2-amino-4-oxo-5-substituted-6-ethylthieno[2,3-
d]pyrimidines as dual thymidylate synthase and dihydrofolate reductase
inhibitors and as potential antitumor agents.";
J. Med. Chem. 52:4892-4902(2009).
[27]
VARIANT DHFRD VAL-153.
PubMed=21310277; DOI=10.1016/j.ajhg.2011.01.007;
Cario H., Smith D.E., Blom H., Blau N., Bode H., Holzmann K.,
Pannicke U., Hopfner K.P., Rump E.M., Ayric Z., Kohne E.,
Debatin K.M., Smulders Y., Schwarz K.;
"Dihydrofolate reductase deficiency due to a homozygous DHFR mutation
causes megaloblastic anemia and cerebral folate deficiency leading to
severe neurologic disease.";
Am. J. Hum. Genet. 88:226-231(2011).
-!- FUNCTION: Key enzyme in folate metabolism. Contributes to the de
novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an
essential reaction for de novo glycine and purine synthesis, and
for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.
{ECO:0000269|PubMed:12096917, ECO:0000269|PubMed:21876188}.
-!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660,
ECO:0000269|PubMed:12096917, ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:17569517, ECO:0000269|PubMed:19196009,
ECO:0000269|PubMed:19478082, ECO:0000269|PubMed:21876184,
ECO:0000269|PubMed:9719595}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.7 uM for dihydrofolate {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009, ECO:0000269|PubMed:21876184};
KM=4.0 uM for NADPH {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009, ECO:0000269|PubMed:21876184};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12657784,
ECO:0000269|PubMed:12925791, ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082,
ECO:0000269|PubMed:2248959, ECO:0000269|PubMed:3383852}.
-!- SUBCELLULAR LOCATION: Mitochondrion
{ECO:0000250|UniProtKB:P00375}. Cytoplasm
{ECO:0000250|UniProtKB:P00375}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00374-1; Sequence=Displayed;
Name=2;
IsoId=P00374-2; Sequence=VSP_056352;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues,
including throughout the fetal and adult brains and whole blood.
Expression is higher in the adult brain than in the fetal brain.
{ECO:0000269|PubMed:21310276}.
-!- DISEASE: Megaloblastic anemia due to dihydrofolate reductase
deficiency (DHFRD) [MIM:613839]: An inborn error of metabolism,
characterized by megaloblastic anemia and/or pancytopenia, severe
cerebral folate deficiency, and cerebral tetrahydrobiopterin
deficiency. Clinical features include variable neurologic
symptoms, ranging from severe developmental delay and generalized
seizures in infancy, to childhood absence epilepsy with learning
difficulties, to lack of symptoms. {ECO:0000269|PubMed:21310276,
ECO:0000269|PubMed:21310277}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the dihydrofolate reductase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Dihydrofolate reductase entry;
URL="https://en.wikipedia.org/wiki/Dihydrofolate_reductase";
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EMBL; J00140; AAA58485.1; -; mRNA.
EMBL; V00507; CAA23765.1; -; mRNA.
EMBL; J00139; AAA58484.1; -; Genomic_DNA.
EMBL; K01612; AAA58484.1; JOINED; Genomic_DNA.
EMBL; K01613; AAA58484.1; JOINED; Genomic_DNA.
EMBL; J00138; AAA58484.1; JOINED; Genomic_DNA.
EMBL; K01614; AAA58484.1; JOINED; Genomic_DNA.
EMBL; X00855; CAA25409.1; -; Genomic_DNA.
EMBL; X00856; CAA25409.1; JOINED; Genomic_DNA.
EMBL; X00857; CAA25409.1; JOINED; Genomic_DNA.
EMBL; X00858; CAA25409.1; JOINED; Genomic_DNA.
EMBL; X00859; CAA25409.1; JOINED; Genomic_DNA.
EMBL; AK293146; BAG56693.1; -; mRNA.
EMBL; AC008434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000192; AAH00192.1; -; mRNA.
EMBL; BC003584; AAH03584.2; -; mRNA.
EMBL; BC070280; AAH70280.1; -; mRNA.
EMBL; BC071996; AAH71996.1; -; mRNA.
CCDS; CCDS47240.1; -. [P00374-1]
CCDS; CCDS78028.1; -. [P00374-2]
PIR; A22551; RDHUD.
RefSeq; NP_000782.1; NM_000791.3. [P00374-1]
RefSeq; NP_001277283.1; NM_001290354.1. [P00374-2]
UniGene; Hs.592364; -.
UniGene; Hs.648635; -.
PDB; 1BOZ; X-ray; 2.10 A; A=2-187.
PDB; 1DHF; X-ray; 2.30 A; A/B=2-187.
PDB; 1DLR; X-ray; 2.30 A; A=2-187.
PDB; 1DLS; X-ray; 2.30 A; A=2-187.
PDB; 1DRF; X-ray; 2.00 A; A=2-187.
PDB; 1HFP; X-ray; 2.10 A; A=2-187.
PDB; 1HFQ; X-ray; 2.10 A; A=2-187.
PDB; 1HFR; X-ray; 2.10 A; A=2-187.
PDB; 1KMS; X-ray; 1.09 A; A=2-187.
PDB; 1KMV; X-ray; 1.05 A; A=2-187.
PDB; 1MVS; X-ray; 1.90 A; A=1-187.
PDB; 1MVT; X-ray; 1.80 A; A=1-187.
PDB; 1OHJ; X-ray; 2.50 A; A=2-187.
PDB; 1OHK; X-ray; 2.50 A; A=2-187.
PDB; 1PD8; X-ray; 2.10 A; A=2-187.
PDB; 1PD9; X-ray; 2.20 A; A=2-187.
PDB; 1PDB; X-ray; 2.20 A; A=2-187.
PDB; 1S3U; X-ray; 2.50 A; A=2-187.
PDB; 1S3V; X-ray; 1.80 A; A=2-187.
PDB; 1S3W; X-ray; 1.90 A; A=2-187.
PDB; 1U71; X-ray; 2.20 A; A=2-187.
PDB; 1U72; X-ray; 1.90 A; A=2-187.
PDB; 1YHO; NMR; -; A=2-187.
PDB; 2C2S; X-ray; 1.40 A; A/B=2-187.
PDB; 2C2T; X-ray; 1.50 A; A/B=2-187.
PDB; 2DHF; X-ray; 2.30 A; A/B=2-187.
PDB; 2W3A; X-ray; 1.50 A; A/B=1-187.
PDB; 2W3B; X-ray; 1.27 A; A/B=1-187.
PDB; 2W3M; X-ray; 1.60 A; A/B=1-187.
PDB; 3EIG; X-ray; 1.70 A; A=2-187.
PDB; 3F8Y; X-ray; 1.45 A; A=1-187.
PDB; 3F8Z; X-ray; 2.01 A; A=1-187.
PDB; 3F91; X-ray; 1.90 A; A=1-187.
PDB; 3FS6; X-ray; 1.23 A; A=1-187.
PDB; 3GHC; X-ray; 1.30 A; A=2-187.
PDB; 3GHV; X-ray; 1.30 A; A=2-187.
PDB; 3GHW; X-ray; 1.24 A; A=2-187.
PDB; 3GI2; X-ray; 1.53 A; A=1-187.
PDB; 3GYF; X-ray; 1.70 A; A=1-187.
PDB; 3L3R; X-ray; 2.00 A; A=2-187.
PDB; 3N0H; X-ray; 1.92 A; A=2-187.
PDB; 3NTZ; X-ray; 1.35 A; A=2-187.
PDB; 3NU0; X-ray; 1.35 A; A=2-187.
PDB; 3NXO; X-ray; 1.35 A; A=2-187.
PDB; 3NXR; X-ray; 1.35 A; A=2-187.
PDB; 3NXT; X-ray; 1.70 A; A=2-187.
PDB; 3NXV; X-ray; 1.90 A; A=2-187.
PDB; 3NXX; X-ray; 1.35 A; A=2-187.
PDB; 3NXY; X-ray; 1.90 A; A=2-187.
PDB; 3NZD; X-ray; 1.80 A; A=2-187.
PDB; 3OAF; X-ray; 1.70 A; A=2-187.
PDB; 3S3V; X-ray; 1.53 A; A=2-187.
PDB; 3S7A; X-ray; 1.80 A; A=2-187.
PDB; 4DDR; X-ray; 2.05 A; A=2-187.
PDB; 4G95; X-ray; 1.35 A; A=2-187.
PDB; 4KAK; X-ray; 1.80 A; A/B=2-187.
PDB; 4KBN; X-ray; 1.84 A; A/B=2-187.
PDB; 4KD7; X-ray; 2.72 A; A/B=2-187.
PDB; 4KEB; X-ray; 1.45 A; A/B=2-187.
PDB; 4KFJ; X-ray; 1.76 A; A/B=2-187.
PDB; 4M6J; X-ray; 1.20 A; A=1-187.
PDB; 4M6K; X-ray; 1.40 A; A=1-187.
PDB; 4M6L; X-ray; 1.70 A; A=1-187.
PDB; 4QHV; X-ray; 1.61 A; A=2-187.
PDB; 4QJC; X-ray; 1.62 A; A=2-187.
PDB; 5HPB; X-ray; 1.65 A; A=2-187.
PDB; 5HQY; X-ray; 1.46 A; A=2-187.
PDB; 5HQZ; X-ray; 1.46 A; A=2-187.
PDB; 5HSR; X-ray; 1.21 A; A=2-187.
PDB; 5HSU; X-ray; 1.46 A; A=2-187.
PDB; 5HT4; X-ray; 1.60 A; A=2-187.
PDB; 5HT5; X-ray; 1.90 A; A=2-187.
PDB; 5HUI; X-ray; 1.46 A; A=2-187.
PDB; 5HVB; X-ray; 1.60 A; A=2-187.
PDB; 5HVE; X-ray; 1.46 A; A=2-187.
PDBsum; 1BOZ; -.
PDBsum; 1DHF; -.
PDBsum; 1DLR; -.
PDBsum; 1DLS; -.
PDBsum; 1DRF; -.
PDBsum; 1HFP; -.
PDBsum; 1HFQ; -.
PDBsum; 1HFR; -.
PDBsum; 1KMS; -.
PDBsum; 1KMV; -.
PDBsum; 1MVS; -.
PDBsum; 1MVT; -.
PDBsum; 1OHJ; -.
PDBsum; 1OHK; -.
PDBsum; 1PD8; -.
PDBsum; 1PD9; -.
PDBsum; 1PDB; -.
PDBsum; 1S3U; -.
PDBsum; 1S3V; -.
PDBsum; 1S3W; -.
PDBsum; 1U71; -.
PDBsum; 1U72; -.
PDBsum; 1YHO; -.
PDBsum; 2C2S; -.
PDBsum; 2C2T; -.
PDBsum; 2DHF; -.
PDBsum; 2W3A; -.
PDBsum; 2W3B; -.
PDBsum; 2W3M; -.
PDBsum; 3EIG; -.
PDBsum; 3F8Y; -.
PDBsum; 3F8Z; -.
PDBsum; 3F91; -.
PDBsum; 3FS6; -.
PDBsum; 3GHC; -.
PDBsum; 3GHV; -.
PDBsum; 3GHW; -.
PDBsum; 3GI2; -.
PDBsum; 3GYF; -.
PDBsum; 3L3R; -.
PDBsum; 3N0H; -.
PDBsum; 3NTZ; -.
PDBsum; 3NU0; -.
PDBsum; 3NXO; -.
PDBsum; 3NXR; -.
PDBsum; 3NXT; -.
PDBsum; 3NXV; -.
PDBsum; 3NXX; -.
PDBsum; 3NXY; -.
PDBsum; 3NZD; -.
PDBsum; 3OAF; -.
PDBsum; 3S3V; -.
PDBsum; 3S7A; -.
PDBsum; 4DDR; -.
PDBsum; 4G95; -.
PDBsum; 4KAK; -.
PDBsum; 4KBN; -.
PDBsum; 4KD7; -.
PDBsum; 4KEB; -.
PDBsum; 4KFJ; -.
PDBsum; 4M6J; -.
PDBsum; 4M6K; -.
PDBsum; 4M6L; -.
PDBsum; 4QHV; -.
PDBsum; 4QJC; -.
PDBsum; 5HPB; -.
PDBsum; 5HQY; -.
PDBsum; 5HQZ; -.
PDBsum; 5HSR; -.
PDBsum; 5HSU; -.
PDBsum; 5HT4; -.
PDBsum; 5HT5; -.
PDBsum; 5HUI; -.
PDBsum; 5HVB; -.
PDBsum; 5HVE; -.
ProteinModelPortal; P00374; -.
SMR; P00374; -.
BioGrid; 108065; 12.
IntAct; P00374; 4.
MINT; MINT-5002355; -.
STRING; 9606.ENSP00000396308; -.
BindingDB; P00374; -.
ChEMBL; CHEMBL202; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB08878; Aminopterin.
DrugBank; DB03886; Biopterin.
DrugBank; DB00798; Gentamicin.
DrugBank; DB00563; Methotrexate.
DrugBank; DB00157; NADH.
DrugBank; DB00642; Pemetrexed.
DrugBank; DB06813; Pralatrexate.
DrugBank; DB01131; Proguanil.
DrugBank; DB00205; Pyrimethamine.
DrugBank; DB03351; Sri-9439.
DrugBank; DB03060; Sri-9662.
DrugBank; DB00440; Trimethoprim.
DrugBank; DB01157; Trimetrexate.
GuidetoPHARMACOLOGY; 2603; -.
MoonProt; P00374; -.
iPTMnet; P00374; -.
PhosphoSitePlus; P00374; -.
SwissPalm; P00374; -.
BioMuta; DHFR; -.
DMDM; 118992; -.
UCD-2DPAGE; P00374; -.
EPD; P00374; -.
MaxQB; P00374; -.
PaxDb; P00374; -.
PeptideAtlas; P00374; -.
PRIDE; P00374; -.
DNASU; 1719; -.
Ensembl; ENST00000439211; ENSP00000396308; ENSG00000228716. [P00374-1]
Ensembl; ENST00000504396; ENSP00000421334; ENSG00000228716. [P00374-2]
Ensembl; ENST00000505337; ENSP00000426474; ENSG00000228716. [P00374-1]
GeneID; 1719; -.
KEGG; hsa:1719; -.
UCSC; uc003kgy.2; human. [P00374-1]
CTD; 1719; -.
DisGeNET; 1719; -.
EuPathDB; HostDB:ENSG00000228716.6; -.
GeneCards; DHFR; -.
HGNC; HGNC:2861; DHFR.
HPA; CAB037129; -.
HPA; HPA051465; -.
MalaCards; DHFR; -.
MIM; 126060; gene.
MIM; 613839; phenotype.
neXtProt; NX_P00374; -.
OpenTargets; ENSG00000228716; -.
Orphanet; 319651; Constitutional megaloblastic anemia with severe neurologic disease.
PharmGKB; PA143; -.
eggNOG; KOG1324; Eukaryota.
eggNOG; COG0262; LUCA.
GeneTree; ENSGT00390000010283; -.
HOGENOM; HOG000040235; -.
HOVERGEN; HBG000773; -.
InParanoid; P00374; -.
KO; K00287; -.
OMA; RDNQLPW; -.
OrthoDB; EOG091G0PRK; -.
PhylomeDB; P00374; -.
TreeFam; TF317636; -.
BRENDA; 1.5.1.3; 2681.
Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-HSA-196757; Metabolism of folate and pterines.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
SABIO-RK; P00374; -.
SIGNOR; P00374; -.
UniPathway; UPA00077; UER00158.
ChiTaRS; DHFR; human.
EvolutionaryTrace; P00374; -.
GeneWiki; Dihydrofolate_reductase; -.
GenomeRNAi; 1719; -.
PRO; PR:P00374; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000228716; -.
CleanEx; HS_DHFR; -.
ExpressionAtlas; P00374; baseline and differential.
Genevisible; P00374; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0004146; F:dihydrofolate reductase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0033560; F:folate reductase activity; TAS:Reactome.
GO; GO:0005542; F:folic acid binding; IDA:BHF-UCL.
GO; GO:0051870; F:methotrexate binding; IDA:BHF-UCL.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0070402; F:NADPH binding; IDA:BHF-UCL.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:CAFA.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:CAFA.
GO; GO:0031103; P:axon regeneration; ISS:BHF-UCL.
GO; GO:0046452; P:dihydrofolate metabolic process; IDA:BHF-UCL.
GO; GO:0046655; P:folic acid metabolic process; ISS:BHF-UCL.
GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
GO; GO:0017148; P:negative regulation of translation; IDA:CAFA.
GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
GO; GO:2000121; P:regulation of removal of superoxide radicals; ISS:BHF-UCL.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0031427; P:response to methotrexate; ISS:BHF-UCL.
GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IMP:BHF-UCL.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IDA:BHF-UCL.
GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:UniProtKB.
CDD; cd00209; DHFR; 1.
Gene3D; 3.40.430.10; -; 1.
InterPro; IPR012259; DHFR.
InterPro; IPR024072; DHFR-like_dom.
InterPro; IPR017925; DHFR_CS.
InterPro; IPR001796; DHFR_dom.
Pfam; PF00186; DHFR_1; 1.
PRINTS; PR00070; DHFR.
SUPFAM; SSF53597; SSF53597; 1.
PROSITE; PS00075; DHFR_1; 1.
PROSITE; PS51330; DHFR_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Methotrexate resistance; Mitochondrion; NADP;
One-carbon metabolism; Oxidoreductase; Reference proteome;
RNA-binding.
CHAIN 1 187 Dihydrofolate reductase.
/FTId=PRO_0000186362.
DOMAIN 4 185 DHFR. {ECO:0000255|PROSITE-
ProRule:PRU00660}.
NP_BIND 16 22 NADP. {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560,
ECO:0000269|PubMed:19478082}.
NP_BIND 55 57 NADP. {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560,
ECO:0000269|PubMed:19478082}.
NP_BIND 77 79 NADP. {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560,
ECO:0000269|PubMed:19478082}.
NP_BIND 117 124 NADP. {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560,
ECO:0000269|PubMed:19478082}.
REGION 31 36 Substrate binding.
{ECO:0000305|PubMed:2248959}.
BINDING 10 10 NADP; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:16222560,
ECO:0000269|PubMed:19478082}.
BINDING 65 65 Substrate. {ECO:0000305|PubMed:2248959}.
BINDING 71 71 Substrate. {ECO:0000305|PubMed:2248959}.
VAR_SEQ 1 52 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056352.
VARIANT 80 80 L -> F (in DHFRD; dbSNP:rs387906619).
{ECO:0000269|PubMed:21310276}.
/FTId=VAR_065818.
VARIANT 153 153 D -> V (in DHFRD; dbSNP:rs121913223).
{ECO:0000269|PubMed:21310277}.
/FTId=VAR_065819.
MUTAGEN 23 23 L->F,W,Y: Decreases affinity for NADP and
dihydrofolate over 10-fold.
{ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:7890613}.
MUTAGEN 23 23 L->R: Strongly decreased affinity for
methotrexate. Decreases catalytic rate
constant 200-fold. Decreases affinity for
NADP and dihydrofolate over 10-fold.
{ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:7890613}.
MUTAGEN 32 32 F->R: Reduces catalytic rate 5-fold.
Reduces affinity for dihydrofolate 9-
fold; when associated with E-36.
{ECO:0000269|PubMed:19478082}.
MUTAGEN 36 36 Q->E: Reduces catalytic rate 2-fold.
Reduces affinity for dihydrofolate 9-
fold; when associated with R-32.
{ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009,
ECO:0000269|PubMed:19478082}.
MUTAGEN 36 36 Q->K: Increases affinity for
dihydrofolate about 3-fold. Reduces
affinity for NADPH about 3-fold.
{ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009,
ECO:0000269|PubMed:19478082}.
MUTAGEN 36 36 Q->S: Increases affinity for
dihydrofolate about 2-fold. No effect on
affinity for NADPH.
{ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009,
ECO:0000269|PubMed:19478082}.
MUTAGEN 65 65 N->F: Increases affinity for
dihydrofolate about 3-fold. No effect on
affinity for NADPH.
{ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009}.
MUTAGEN 65 65 N->S: Increases affinity for
dihydrofolate about 15-fold. No effect on
affinity for NADPH.
{ECO:0000269|PubMed:15039552,
ECO:0000269|PubMed:19196009}.
CONFLICT 113 113 V -> L (in Ref. 6; AAH70280).
{ECO:0000305}.
STRAND 5 11 {ECO:0000244|PDB:1KMV}.
STRAND 16 19 {ECO:0000244|PDB:1KMV}.
STRAND 24 26 {ECO:0000244|PDB:5HVE}.
HELIX 29 40 {ECO:0000244|PDB:1KMV}.
STRAND 43 46 {ECO:0000244|PDB:5HQY}.
STRAND 48 54 {ECO:0000244|PDB:1KMV}.
HELIX 55 60 {ECO:0000244|PDB:1KMV}.
HELIX 63 65 {ECO:0000244|PDB:1KMV}.
STRAND 71 76 {ECO:0000244|PDB:1KMV}.
STRAND 88 93 {ECO:0000244|PDB:1KMV}.
HELIX 94 101 {ECO:0000244|PDB:1KMV}.
TURN 104 109 {ECO:0000244|PDB:1KMV}.
STRAND 110 115 {ECO:0000244|PDB:1KMV}.
HELIX 119 126 {ECO:0000244|PDB:1KMV}.
STRAND 128 130 {ECO:0000244|PDB:4M6K}.
STRAND 132 141 {ECO:0000244|PDB:1KMV}.
STRAND 146 148 {ECO:0000244|PDB:1KMV}.
TURN 154 156 {ECO:0000244|PDB:1KMV}.
STRAND 157 159 {ECO:0000244|PDB:1KMS}.
STRAND 161 163 {ECO:0000244|PDB:3S7A}.
STRAND 171 173 {ECO:0000244|PDB:1KMV}.
STRAND 176 185 {ECO:0000244|PDB:1KMV}.
SEQUENCE 187 AA; 21453 MW; EBDF3D1EC73E1566 CRC64;
MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS
IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS
VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF
EVYEKND


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