UniProtKB - P00374 (DYR_HUMAN)
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- BLAST>sp|P00374|DYR_HUMAN Dihydrofolate reductase OS=Homo sapiens OX=9606 GN=DHFR PE=1 SV=2 MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF EVYEKND
- Align
Dihydrofolate reductase
DHFR
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria."
Anderson D.D., Quintero C.M., Stover P.J.
Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.17"Atomic structures of human dihydrofolate reductase complexed with NADPH and two lipophilic antifolates at 1.09 A and 1.05 A resolution."
Klon A.E., Heroux A., Ross L.J., Pathak V., Johnson C.A., Piper J.R., Borhani D.W.
J. Mol. Biol. 320:677-693(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEXES WITH NADP AND THE SYNTHETIC INHIBITORS SRI-9439 AND SRI-9662, FUNCTION, CATALYTIC ACTIVITY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
7 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The former annotated human pseudogene dihydrofolate reductase-like 1 (DHFRL1) is expressed and functional."
McEntee G., Minguzzi S., O'Brien K., Ben Larbi N., Loscher C., O'Fagain C., Parle-McDermott A.
Proc. Natl. Acad. Sci. U.S.A. 108:15157-15162(2011) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, RNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.16"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."
Gangjee A., Vidwans A.P., Vasudevan A., Queener S.F., Kisliuk R.L., Cody V., Li R., Galitsky N., Luft J.R., Pangborn W.
J. Med. Chem. 41:3426-3434(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH NADPH AND QUINAZOLINE INHIBITORS, CATALYTIC ACTIVITY. - Ref.17"Atomic structures of human dihydrofolate reductase complexed with NADPH and two lipophilic antifolates at 1.09 A and 1.05 A resolution."
Klon A.E., Heroux A., Ross L.J., Pathak V., Johnson C.A., Piper J.R., Borhani D.W.
J. Mol. Biol. 320:677-693(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEXES WITH NADP AND THE SYNTHETIC INHIBITORS SRI-9439 AND SRI-9662, FUNCTION, CATALYTIC ACTIVITY. - Ref.20"Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry."
Cody V., Luft J.R., Pangborn W., Gangjee A., Queener S.F.
Acta Crystallogr. D 60:646-655(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR, MUTAGENESIS OF GLN-36 AND ASN-65, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.23"Novel boron-containing, nonclassical antifolates: synthesis and preliminary biological and structural evaluation."
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.
J. Med. Chem. 50:3283-3289(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEXES WITH NADP AND BORON-CONTAINING INHIBITORS, CATALYTIC ACTIVITY. - Ref.24"Correlations of inhibitor kinetics for Pneumocystis jirovecii and human dihydrofolate reductase with structural data for human active site mutant enzyme complexes."
Cody V., Pace J., Makin J., Piraino J., Queener S.F., Rosowsky A.
Biochemistry 48:1702-1711(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEXES WITH NADP AND THE SYNTHETIC INHIBITOR PY957, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-36 AND ASN-65. - Ref.25"Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance."
Volpato J.P., Yachnin B.J., Blanchet J., Guerrero V., Poulin L., Fossati E., Berghuis A.M., Pelletier J.N.
J. Biol. Chem. 284:20079-20089(2009) [PubMed] [Europe PMC] [Abstract]Cited for: 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, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=2.7 µM for dihydrofolate3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The former annotated human pseudogene dihydrofolate reductase-like 1 (DHFRL1) is expressed and functional."
McEntee G., Minguzzi S., O'Brien K., Ben Larbi N., Loscher C., O'Fagain C., Parle-McDermott A.
Proc. Natl. Acad. Sci. U.S.A. 108:15157-15162(2011) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, RNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry."
Cody V., Luft J.R., Pangborn W., Gangjee A., Queener S.F.
Acta Crystallogr. D 60:646-655(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR, MUTAGENESIS OF GLN-36 AND ASN-65, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.24"Correlations of inhibitor kinetics for Pneumocystis jirovecii and human dihydrofolate reductase with structural data for human active site mutant enzyme complexes."
Cody V., Pace J., Makin J., Piraino J., Queener S.F., Rosowsky A.
Biochemistry 48:1702-1711(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEXES WITH NADP AND THE SYNTHETIC INHIBITOR PY957, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-36 AND ASN-65.
- KM=4.0 µM for NADPH3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The former annotated human pseudogene dihydrofolate reductase-like 1 (DHFRL1) is expressed and functional."
McEntee G., Minguzzi S., O'Brien K., Ben Larbi N., Loscher C., O'Fagain C., Parle-McDermott A.
Proc. Natl. Acad. Sci. U.S.A. 108:15157-15162(2011) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, RNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry."
Cody V., Luft J.R., Pangborn W., Gangjee A., Queener S.F.
Acta Crystallogr. D 60:646-655(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR, MUTAGENESIS OF GLN-36 AND ASN-65, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.24"Correlations of inhibitor kinetics for Pneumocystis jirovecii and human dihydrofolate reductase with structural data for human active site mutant enzyme complexes."
Cody V., Pace J., Makin J., Piraino J., Queener S.F., Rosowsky A.
Biochemistry 48:1702-1711(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEXES WITH NADP AND THE SYNTHETIC INHIBITOR PY957, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-36 AND ASN-65.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.Proteins known to be involved in this subpathway in this organism are:
- Dihydrofolate reductase 2, mitochondrial (DHFR2), Dihydrofolate reductase (DHFR)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 10 | NADP; via amide nitrogen and carbonyl oxygen3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 65 | Substrate1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 71 | Substrate1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 16 – 22 | NADP3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 7 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 55 – 57 | NADP3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 77 – 79 | NADP3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 117 – 124 | NADP3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 8 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- dihydrofolate reductase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- drug binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- folate reductase activity Source: Reactome
- folic acid binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- methotrexate binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- NADPH binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- sequence-specific mRNA binding Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- translation repressor activity, mRNA regulatory element binding Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- axon regeneration Source: BHF-UCL
- dihydrofolate metabolic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- folic acid metabolic process Source: BHF-UCL
- negative regulation of translation Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- one-carbon metabolic process Source: UniProtKB-KW
- oxidation-reduction process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of nitric-oxide synthase activity Source: BHF-UCL
- regulation of removal of superoxide radicals Source: BHF-UCL
- regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
- response to methotrexate Source: BHF-UCL
- tetrahydrobiopterin biosynthetic process Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- tetrahydrofolate biosynthetic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- tetrahydrofolate metabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Oxidoreductase, RNA-binding |
| Biological process | Methotrexate resistance, One-carbon metabolism |
| Ligand | NADP |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS09699-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.5.1.3 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-196757 Metabolism of folate and pterines R-HSA-539107 Activation of E2F1 target genes at G1/S |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00374 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P00374 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00077; UER00158 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P00374 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:DHFR |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000228716.6 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2861 DHFR |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 126060 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P00374 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Mitochondrion
- Mitochondrion By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Mitochondrion By similarity
Other locations
- Cytoplasm By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Cytoplasm By similarity
Cytosol
- cytosol Source: Reactome
Mitochondrion
- mitochondrion Source: HPA
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Mitochondrion<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Megaloblastic anemia due to dihydrofolate reductase deficiency (DHFRD)2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.7"Identification and characterization of an inborn error of metabolism caused by dihydrofolate reductase deficiency."
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.
Am. J. Hum. Genet. 88:216-225(2011) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, VARIANT DHFRD PHE-80. - Ref.27"Dihydrofolate reductase deficiency due to a homozygous DHFR mutation causes megaloblastic anemia and cerebral folate deficiency leading to severe neurologic disease."
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.
Am. J. Hum. Genet. 88:226-231(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT DHFRD VAL-153.
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.
Am. J. Hum. Genet. 88:216-225(2011) [PubMed] [Europe PMC] [Abstract]
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.
Am. J. Hum. Genet. 88:226-231(2011) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065818 | 80 | L → F in DHFRD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065819 | 153 | D → V in DHFRD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 23 | L → F, W or Y: Decreases affinity for NADP and dihydrofolate over 10-fold. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 23 | L → R: Strongly decreased affinity for methotrexate. Decreases catalytic rate constant 200-fold. Decreases affinity for NADP and dihydrofolate over 10-fold. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 32 | F → R: Reduces catalytic rate 5-fold. Reduces affinity for dihydrofolate 9-fold; when associated with E-36. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 36 | Q → E: Reduces catalytic rate 2-fold. Reduces affinity for dihydrofolate 9-fold; when associated with R-32. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 36 | Q → K: Increases affinity for dihydrofolate about 3-fold. Reduces affinity for NADPH about 3-fold. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 36 | Q → S: Increases affinity for dihydrofolate about 2-fold. No effect on affinity for NADPH. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 65 | N → F: Increases affinity for dihydrofolate about 3-fold. No effect on affinity for NADPH. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 65 | N → S: Increases affinity for dihydrofolate about 15-fold. No effect on affinity for NADPH. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 1719 |
MalaCards human disease database More...MalaCardsi | DHFR |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613839 phenotype |
Open Targets More...OpenTargetsi | ENSG00000228716 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 319651 Constitutional megaloblastic anemia with severe neurologic disease |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA143 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL202 |
Drug and drug target database More...DrugBanki | DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose DB08878 Aminopterin DB03886 Biopterin DB00798 Gentamicin DB00563 Methotrexate DB00157 NADH DB00642 Pemetrexed DB06813 Pralatrexate DB01131 Proguanil DB00205 Pyrimethamine DB03351 Sri-9439 DB03060 Sri-9662 DB00440 Trimethoprim DB01157 Trimetrexate |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2603 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DHFR |
Domain mapping of disease mutations (DMDM) More...DMDMi | 118992 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000186362 | 1 – 187 | Dihydrofolate reductaseAdd BLAST | 187 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P00374 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P00374 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00374 |
PeptideAtlas More...PeptideAtlasi | P00374 |
PRoteomics IDEntifications database More...PRIDEi | P00374 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51237 |
2D gel databases
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P00374 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P00374 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P00374 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P00374 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Identification and characterization of an inborn error of metabolism caused by dihydrofolate reductase deficiency."
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.
Am. J. Hum. Genet. 88:216-225(2011) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, VARIANT DHFRD PHE-80.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000228716 |
CleanEx database of gene expression profiles More...CleanExi | HS_DHFR |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P00374 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P00374 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB037129 HPA051465 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Crystal structure of human dihydrofolate reductase complexed with folate."
Oefner C., D'Arcy A., Winkler F.K.
Eur. J. Biochem. 174:377-385(1988) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FOLATE. - Ref.12"Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate."
Davies J.F., Delcamp T.J., Prendergast N.J., Ashford V.A., Freisheim J.H., Kraut J.
Biochemistry 29:9467-9479(1990) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH FOLATE AND 5-DEAZAFOLATE, SUBUNIT. - Ref.18"Analysis of two polymorphic forms of a pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolate binary complex with human dihydrofolate reductase."
Cody V., Galitsky N., Luft J.R., Pangborn W., Gangjee A.
Acta Crystallogr. D 59:654-661(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR. - Ref.19"Analysis of three crystal structure determinations of a 5-methyl-6-N-methylanilino pyridopyrimidine antifolate complex with human dihydrofolate reductase."
Cody V., Luft J.R., Pangborn W., Gangjee A.
Acta Crystallogr. D 59:1603-1609(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR. - Ref.20"Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry."
Cody V., Luft J.R., Pangborn W., Gangjee A., Queener S.F.
Acta Crystallogr. D 60:646-655(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR, MUTAGENESIS OF GLN-36 AND ASN-65, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.22"Solution structure of human dihydrofolate reductase in its complex with trimethoprim and NADPH."
Kovalevskaya N.V., Smurnyy Y.D., Polshakov V.I., Birdsall B., Bradbury A.F., Frenkiel T., Feeney J.
J. Biomol. NMR 33:69-72(2005) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR IN COMPLEX WITH TRIMETHOPRIM AND NADPH. - Ref.25"Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance."
Volpato J.P., Yachnin B.J., Blanchet J., Guerrero V., Poulin L., Fossati E., Berghuis A.M., Pelletier J.N.
J. Biol. Chem. 284:20079-20089(2009) [PubMed] [Europe PMC] [Abstract]Cited for: 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, CATALYTIC ACTIVITY.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108065, 16 interactors |
Protein interaction database and analysis system More...IntActi | P00374, 5 interactors |
Molecular INTeraction database More...MINTi | P00374 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000396308 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00374 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 11 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 16 – 19 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 24 – 26 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 29 – 40 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 43 – 46 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 48 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 55 – 60 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 63 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 71 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 88 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 94 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 104 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 110 – 115 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 119 – 126 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 128 – 130 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 132 – 141 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 146 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 154 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 157 – 159 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 161 – 163 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 171 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 176 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P00374 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00374 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00374 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 4 – 185 | DHFRPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 182 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 31 – 36 | Substrate binding1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 6 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1324 Eukaryota COG0262 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000010283 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000040235 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000773 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00374 |
KEGG Orthology (KO) More...KOi | K00287 |
Identification of Orthologs from Complete Genome Data More...OMAi | RDNQLPW |
Database of Orthologous Groups More...OrthoDBi | EOG091G0PRK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P00374 |
TreeFam database of animal gene trees More...TreeFami | TF317636 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00209 DHFR, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.430.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR024072 DHFR-like_dom_sf IPR017925 DHFR_CS IPR001796 DHFR_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00186 DHFR_1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53597 SSF53597, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL
60 70 80 90 100
VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL
110 120 130 140 150
TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP
160 170 180
EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND
The sequence of this isoform differs from the canonical sequence as follows:
1-52: Missing.
10 20 30 40 50
MGKKTWFSIP EKNRPLKGRI NLVLSRELKE PPQGAHFLSR SLDDALKLTE
60 70 80 90 100
QPELANKVDM VWIVGGSSVY KEAMNHPGHL KLFVTRIMQD FESDTFFPEI
110 120 130
DLEKYKLLPE YPGVLSDVQE EKGIKYKFEV YEKND
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 113 | V → L in AAH70280 (PubMed:15489334).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065818 | 80 | L → F in DHFRD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065819 | 153 | D → V in DHFRD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J00140 mRNA Translation: AAA58485.1 V00507 mRNA Translation: CAA23765.1 J00139 , K01612, K01613, J00138, K01614 Genomic DNA Translation: AAA58484.1 X00855 , X00856, X00857, X00858, X00859 Genomic DNA Translation: CAA25409.1 AK293146 mRNA Translation: BAG56693.1 AC008434 Genomic DNA No translation available. AC010270 Genomic DNA No translation available. BC000192 mRNA Translation: AAH00192.1 BC003584 mRNA Translation: AAH03584.2 BC070280 mRNA Translation: AAH70280.1 BC071996 mRNA Translation: AAH71996.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47240.1 [P00374-1] CCDS78028.1 [P00374-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A22551 RDHUD |
NCBI Reference Sequences More...RefSeqi | NP_000782.1, NM_000791.3 [P00374-1] NP_001277283.1, NM_001290354.1 [P00374-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.592364 Hs.648635 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000439211; ENSP00000396308; ENSG00000228716 [P00374-1] ENST00000504396; ENSP00000421334; ENSG00000228716 [P00374-2] ENST00000505337; ENSP00000426474; ENSG00000228716 [P00374-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1719 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1719 |
UCSC genome browser More...UCSCi | uc003kgy.2 human [P00374-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00374 | Dihydrofolate reductase | 187 | |||
| Trimethoprim resistant protein | 187 | ||||
| Trimethoprim resistant protein | 187 | ||||
| Dihydrofolate reductase, isoform CRA_a | 262 | ||||
| UPI0000110FCE | 186 | ||||
| P00374-2 | Dihydrofolate reductase/Cytidine and deoxycytidylate deaminase zinc-binding region/Uracil phosphoribosyltransferase, putative | 559 | |||
| Fur1p | 142 | ||||
| Fcy1p | 153 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00374 | Dihydrofolate reductase | 187 | |||
| Trimethoprim resistant protein | 187 | ||||
| Trimethoprim resistant protein | 187 | ||||
| UPI000D31DFB4 | 262 | ||||
| UPI00045DBAC7 | 241 | ||||
| +20 | |||||
| P00374-2 | Dihydrofolate reductase/Cytidine and deoxycytidylate deaminase zinc-binding region/Uracil phosphoribosyltransferase, putative | 559 | |||
| Fur1p | 142 | ||||
| Fcy1p | 153 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00374 | Dihydrofolate reductase | 187 | |||
| Trimethoprim resistant protein | 187 | ||||
| Trimethoprim resistant protein | 187 | ||||
| UPI000D31DFB4 | 262 | ||||
| UPI00045DBAC7 | 241 | ||||
| +24 | |||||
| P00374-2 | Dihydrofolate reductase/Cytidine and deoxycytidylate deaminase zinc-binding region/Uracil phosphoribosyltransferase, putative | 559 | |||
| Fur1p | 142 | ||||
| Fcy1p | 153 | ||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Dihydrofolate reductase entry |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J00140 mRNA Translation: AAA58485.1 V00507 mRNA Translation: CAA23765.1 J00139 , K01612, K01613, J00138, K01614 Genomic DNA Translation: AAA58484.1 X00855 , X00856, X00857, X00858, X00859 Genomic DNA Translation: CAA25409.1 AK293146 mRNA Translation: BAG56693.1 AC008434 Genomic DNA No translation available. AC010270 Genomic DNA No translation available. BC000192 mRNA Translation: AAH00192.1 BC003584 mRNA Translation: AAH03584.2 BC070280 mRNA Translation: AAH70280.1 BC071996 mRNA Translation: AAH71996.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47240.1 [P00374-1] CCDS78028.1 [P00374-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A22551 RDHUD |
NCBI Reference Sequences More...RefSeqi | NP_000782.1, NM_000791.3 [P00374-1] NP_001277283.1, NM_001290354.1 [P00374-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.592364 Hs.648635 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1BOZ | X-ray | 2.10 | A | 2-187 | [»] | |
| 1DHF | X-ray | 2.30 | A/B | 2-187 | [»] | |
| 1DLR | X-ray | 2.30 | A | 2-187 | [»] | |
| 1DLS | X-ray | 2.30 | A | 2-187 | [»] | |
| 1DRF | X-ray | 2.00 | A | 2-187 | [»] | |
| 1HFP | X-ray | 2.10 | A | 2-187 | [»] | |
| 1HFQ | X-ray | 2.10 | A | 2-187 | [»] | |
| 1HFR | X-ray | 2.10 | A | 2-187 | [»] | |
| 1KMS | X-ray | 1.09 | A | 2-187 | [»] | |
| 1KMV | X-ray | 1.05 | A | 2-187 | [»] | |
| 1MVS | X-ray | 1.90 | A | 1-187 | [»] | |
| 1MVT | X-ray | 1.80 | A | 1-187 | [»] | |
| 1OHJ | X-ray | 2.50 | A | 2-187 | [»] | |
| 1OHK | X-ray | 2.50 | A | 2-187 | [»] | |
| 1PD8 | X-ray | 2.10 | A | 2-187 | [»] | |
| 1PD9 | X-ray | 2.20 | A | 2-187 | [»] | |
| 1PDB | X-ray | 2.20 | A | 2-187 | [»] | |
| 1S3U | X-ray | 2.50 | A | 2-187 | [»] | |
| 1S3V | X-ray | 1.80 | A | 2-187 | [»] | |
| 1S3W | X-ray | 1.90 | A | 2-187 | [»] | |
| 1U71 | X-ray | 2.20 | A | 2-187 | [»] | |
| 1U72 | X-ray | 1.90 | A | 2-187 | [»] | |
| 1YHO | NMR | - | A | 2-187 | [»] | |
| 2C2S | X-ray | 1.40 | A/B | 2-187 | [»] | |
| 2C2T | X-ray | 1.50 | A/B | 2-187 | [»] | |
| 2DHF | X-ray | 2.30 | A/B | 2-187 | [»] | |
| 2W3A | X-ray | 1.50 | A/B | 1-187 | [»] | |
| 2W3B | X-ray | 1.27 | A/B | 1-187 | [»] | |
| 2W3M | X-ray | 1.60 | A/B | 1-187 | [»] | |
| 3EIG | X-ray | 1.70 | A | 2-187 | [»] | |
| 3F8Y | X-ray | 1.45 | A | 1-187 | [»] | |
| 3F8Z | X-ray | 2.01 | A | 1-187 | [»] | |
| 3F91 | X-ray | 1.90 | A | 1-187 | [»] | |
| 3FS6 | X-ray | 1.23 | A | 1-187 | [»] | |
| 3GHC | X-ray | 1.30 | A | 2-187 | [»] | |
| 3GHV | X-ray | 1.30 | A | 2-187 | [»] | |
| 3GHW | X-ray | 1.24 | A | 2-187 | [»] | |
| 3GI2 | X-ray | 1.53 | A | 1-187 | [»] | |
| 3GYF | X-ray | 1.70 | A | 1-187 | [»] | |
| 3L3R | X-ray | 2.00 | A | 2-187 | [»] | |
| 3N0H | X-ray | 1.92 | A | 2-187 | [»] | |
| 3NTZ | X-ray | 1.35 | A | 2-187 | [»] | |
| 3NU0 | X-ray | 1.35 | A | 2-187 | [»] | |
| 3NXO | X-ray | 1.35 | A | 2-187 | [»] | |
| 3NXR | X-ray | 1.35 | A | 2-187 | [»] | |
| 3NXT | X-ray | 1.70 | A | 2-187 | [»] | |
| 3NXV | X-ray | 1.90 | A | 2-187 | [»] | |
| 3NXX | X-ray | 1.35 | A | 2-187 | [»] | |
| 3NXY | X-ray | 1.90 | A | 2-187 | [»] | |
| 3NZD | X-ray | 1.80 | A | 2-187 | [»] | |
| 3OAF | X-ray | 1.70 | A | 2-187 | [»] | |
| 3S3V | X-ray | 1.53 | A | 2-187 | [»] | |
| 3S7A | X-ray | 1.80 | A | 2-187 | [»] | |
| 4DDR | X-ray | 2.05 | A | 2-187 | [»] | |
| 4G95 | X-ray | 1.35 | A | 2-187 | [»] | |
| 4KAK | X-ray | 1.80 | A/B | 2-187 | [»] | |
| 4KBN | X-ray | 1.84 | A/B | 2-187 | [»] | |
| 4KD7 | X-ray | 2.72 | A/B | 2-187 | [»] | |
| 4KEB | X-ray | 1.45 | A/B | 2-187 | [»] | |
| 4KFJ | X-ray | 1.76 | A/B | 2-187 | [»] | |
| 4M6J | X-ray | 1.20 | A | 1-187 | [»] | |
| 4M6K | X-ray | 1.40 | A | 1-187 | [»] | |
| 4M6L | X-ray | 1.70 | A | 1-187 | [»] | |
| 4QHV | X-ray | 1.61 | A | 2-187 | [»] | |
| 4QJC | X-ray | 1.62 | A | 2-187 | [»] | |
| 5HPB | X-ray | 1.65 | A | 2-187 | [»] | |
| 5HQY | X-ray | 1.46 | A | 2-187 | [»] | |
| 5HQZ | X-ray | 1.46 | A | 2-187 | [»] | |
| 5HSR | X-ray | 1.21 | A | 2-187 | [»] | |
| 5HSU | X-ray | 1.46 | A | 2-187 | [»] | |
| 5HT4 | X-ray | 1.60 | A | 2-187 | [»] | |
| 5HT5 | X-ray | 1.90 | A | 2-187 | [»] | |
| 5HUI | X-ray | 1.46 | A | 2-187 | [»] | |
| 5HVB | X-ray | 1.60 | A | 2-187 | [»] | |
| 5HVE | X-ray | 1.46 | A | 2-187 | [»] | |
| 6DAV | X-ray | 1.55 | A/B | 1-187 | [»] | |
| 6DE4 | X-ray | 2.41 | A/B | 2-187 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P00374 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00374 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108065, 16 interactors |
Protein interaction database and analysis system More...IntActi | P00374, 5 interactors |
Molecular INTeraction database More...MINTi | P00374 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000396308 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00374 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL202 |
Drug and drug target database More...DrugBanki | DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose DB08878 Aminopterin DB03886 Biopterin DB00798 Gentamicin DB00563 Methotrexate DB00157 NADH DB00642 Pemetrexed DB06813 Pralatrexate DB01131 Proguanil DB00205 Pyrimethamine DB03351 Sri-9439 DB03060 Sri-9662 DB00440 Trimethoprim DB01157 Trimetrexate |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2603 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P00374 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P00374 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P00374 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P00374 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DHFR |
Domain mapping of disease mutations (DMDM) More...DMDMi | 118992 |
2D gel databases
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P00374 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P00374 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P00374 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00374 |
PeptideAtlas More...PeptideAtlasi | P00374 |
PRoteomics IDEntifications database More...PRIDEi | P00374 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51237 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1719 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000439211; ENSP00000396308; ENSG00000228716 [P00374-1] ENST00000504396; ENSP00000421334; ENSG00000228716 [P00374-2] ENST00000505337; ENSP00000426474; ENSG00000228716 [P00374-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1719 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1719 |
UCSC genome browser More...UCSCi | uc003kgy.2 human [P00374-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1719 |
DisGeNET More...DisGeNETi | 1719 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000228716.6 |
GeneCards: human genes, protein and diseases More...GeneCardsi | DHFR |
Human Gene Nomenclature Database More...HGNCi | HGNC:2861 DHFR |
Human Protein Atlas More...HPAi | CAB037129 HPA051465 |
MalaCards human disease database More...MalaCardsi | DHFR |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 126060 gene 613839 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P00374 |
Open Targets More...OpenTargetsi | ENSG00000228716 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 319651 Constitutional megaloblastic anemia with severe neurologic disease |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA143 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1324 Eukaryota COG0262 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000010283 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000040235 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000773 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00374 |
KEGG Orthology (KO) More...KOi | K00287 |
Identification of Orthologs from Complete Genome Data More...OMAi | RDNQLPW |
Database of Orthologous Groups More...OrthoDBi | EOG091G0PRK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P00374 |
TreeFam database of animal gene trees More...TreeFami | TF317636 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00077; UER00158 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS09699-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.5.1.3 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-196757 Metabolism of folate and pterines R-HSA-539107 Activation of E2F1 target genes at G1/S |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00374 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P00374 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | DHFR human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00374 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Dihydrofolate_reductase |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1719 |
Protein Ontology More...PROi | PR:P00374 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000228716 |
CleanEx database of gene expression profiles More...CleanExi | HS_DHFR |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P00374 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P00374 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00209 DHFR, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.430.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR024072 DHFR-like_dom_sf IPR017925 DHFR_CS IPR001796 DHFR_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00186 DHFR_1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53597 SSF53597, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | DYR_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P00374Primary (citable) accession number: P00374 Secondary accession number(s): B4DDD2, Q14130, Q6IRW8 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 202 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
