methylenetetrahydrofolate reductase

mammalian protein found in Homo sapiens
Protein protein Q424709
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Summary

methylenetetrahydrofolate reductase is a protein[1]. It ranks in the top 5% of protein entities by monthly Wikipedia readership (638 views/month).[2]

Key Facts

  • methylenetetrahydrofolate reductase's instance of is recorded as protein[3].
  • methylenetetrahydrofolate reductase is a type of enzyme[4].
  • methylenetetrahydrofolate reductase is part of FAD-linked oxidoreductase-like[5].
  • methylenetetrahydrofolate reductase is part of Eukaryotic-type methylenetetrahydrofolate reductase[6].
  • methylenetetrahydrofolate reductase's Commons category is recorded as Methylenetetrahydrofolate reductase[7].
  • methylenetetrahydrofolate reductase's molecular function is recorded as flavin adenine dinucleotide binding[8].
  • methylenetetrahydrofolate reductase's molecular function is recorded as methylenetetrahydrofolate reductase (NAD(P)H) activity[9].
  • methylenetetrahydrofolate reductase's molecular function is recorded as modified amino acid binding[10].
  • methylenetetrahydrofolate reductase's molecular function is recorded as catalytic activity[11].
  • methylenetetrahydrofolate reductase's molecular function is recorded as NADP binding[12].
  • methylenetetrahydrofolate reductase's molecular function is recorded as oxidoreductase activity[13].
  • methylenetetrahydrofolate reductase's molecular function is recorded as protein-containing complex binding[14].
  • methylenetetrahydrofolate reductase's cell component is recorded as cytosol[15].
  • methylenetetrahydrofolate reductase's cell component is recorded as synapse[16].
  • methylenetetrahydrofolate reductase's biological process is recorded as response to amino acid[17].
  • methylenetetrahydrofolate reductase's biological process is recorded as response to interleukin-1[18].
  • methylenetetrahydrofolate reductase's biological process is recorded as response to hypoxia[19].
  • methylenetetrahydrofolate reductase's biological process is recorded as cellular amino acid metabolic process[20].
  • methylenetetrahydrofolate reductase's biological process is recorded as tetrahydrofolate interconversion[21].
  • methylenetetrahydrofolate reductase's biological process is recorded as S-adenosylmethionine metabolic process[22].
  • methylenetetrahydrofolate reductase's biological process is recorded as blood circulation[23].
  • methylenetetrahydrofolate reductase's biological process is recorded as tetrahydrofolate metabolic process[24].
  • methylenetetrahydrofolate reductase's biological process is recorded as methionine metabolic process[25].
  • methylenetetrahydrofolate reductase's biological process is recorded as regulation of histone methylation[26].
  • methylenetetrahydrofolate reductase's biological process is recorded as response to vitamin B2[27].

Why It Matters

methylenetetrahydrofolate reductase ranks in the top 5% of protein entities by monthly Wikipedia readership (638 views/month).[2] It has Wikipedia articles in 13 language editions, a strong signal of global cultural recognition.[28] It is known by 17 alternative names across languages and contexts.[29]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] ↑ . UniProt. Retrieved . wikidata.org.
  2. [4] ↑ . wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . wikidata.org.
  6. [8] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . Novel associations of CPS1, MUT, NOX4, and DPEP1 with plasma homocysteine in a healthy population: a genome-wide evaluation of 13 974 participants in the Women's Genome Health Study. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . MTHFR promotes heterochromatin maintenance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . Insights into severe 5,10-methylenetetrahydrofolate reductase deficiency: molecular genetic and enzymatic characterization of 76 patients. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . Functional characterization of human methylenetetrahydrofolate reductase in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . MTHFR promotes heterochromatin maintenance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikimedia Foundation. dumps.wikimedia.org.
  2. [28] ↑ . Wikidata sitelinks. wikidata.org.
  3. [29] ↑ . Wikidata aliases. wikidata.org.

📑 Cite this page

Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). methylenetetrahydrofolate reductase. Retrieved October 16, 2026, from https://4ort.xyz/entity/methylenetetrahydrofolate-reductase
MLA “methylenetetrahydrofolate reductase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 16 Oct. 2026, https://4ort.xyz/entity/methylenetetrahydrofolate-reductase.
BibTeX @misc{4ortxyz_methylenetetrahydrofolate-reductase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{methylenetetrahydrofolate reductase}}, year = {2026}, url = {https://4ort.xyz/entity/methylenetetrahydrofolate-reductase}, note = {Accessed: 2026-10-16}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): methylenetetrahydrofolate reductase — https://4ort.xyz/entity/methylenetetrahydrofolate-reductase (retrieved 2026-10-16)

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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 12w ago · Boghog · 2026-07-23 view diff on Wikidata ↗
    Instance of → —
    Part of → —
    Subclass of → enzyme
    Encoded by → MTHFR
    + 9 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 1.5.1.53, [[:toollabs:quickstatements/#/batch/261446|batch #261446]]"
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