MTHFD2 - XIV

Protein-coding gene in the: species Homo sapiens

MTHFD2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1ZN4

Identifiers

Aliases

MTHFD2, NMDMC, methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase

External IDs

OMIM: 604887; MGI: 1338850; HomoloGene: 21321; GeneCards: MTHFD2; OMA:MTHFD2 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)

Band	2p13.1	Start	74,186,172 bp
Band	2p13.1	End	74,217,565 bp

Gene location (Mouse)

Chr.	Chromosome 6 (mouse)

Band	6 C3\|6 35.94 cM	Start	83,282,673 bp
Band	6 C3\|6 35.94 cM	End	83,302,890 bp

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

cartilage tissue

Descending thoracic aorta

popliteal artery

tibial arteries

ascending aorta

gonad

left coronary artery

right coronary artery

stromal cell of endometrium

tibia

Top expressed in

lacrimal gland

seminal vesicula

Ileal epithelium

zygote

calvaria

secondary oocyte

primary oocyte

primitive streak

Paneth cell

salivary gland

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	oxidoreductase activity catalytic activity hydrolase activity methenyltetrahydrofolate cyclohydrolase activity magnesium ion binding methylenetetrahydrofolate dehydrogenase (NAD+) activity methylenetetrahydrofolate dehydrogenase (NADP+) activity phosphate ion binding
Cellular component	mitochondrion cytosol mitochondrial matrix extracellular space
Biological process	metabolism one-carbon metabolic process tetrahydrofolate metabolic process folic acid metabolic process tetrahydrofolate interconversion
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


10797


17768

Ensembl


ENSG00000065911


ENSMUSG00000005667

UniProt


P13995


P18155

RefSeq (mRNA)


NM_001040409 NM_006636


NM_008638

RefSeq (protein)


NP_006627


NP_032664

Location (UCSC)

Chr 2: 74.19 – 74.22 Mb

Chr 6: 83.28 – 83.3 Mb

PubMed search

Wikidata

View/Edit Human

View/Edit Mouse

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial is: an enzyme that in humans is encoded by, the——MTHFD2 gene.

This gene encodes a nuclear-encoded mitochondrial bifunctional enzyme with methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. The enzyme functions as a homodimer and is unique in its absolute requirement for magnesium and inorganic phosphate. Formation of the "enzyme-magnesium complex allows binding of NAD." Alternative splicing results in multiple transcripts encoding different isoforms. This gene has a pseudogene on chromosome 7.

References※

^ GRCh38: Ensembl release 89: ENSG00000065911 – Ensembl, May 2017
^ GRCm38: Ensembl release 89: ENSMUSG00000005667 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, "U."S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, "U."S. National Library of Medicine.
^ Peri KG, Belanger C, Mackenzie RE (Dec 1989). "Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase". Nucleic Acids Res. 17 (21): 8853. doi:10.1093/nar/17.21.8853. PMC 335047. PMID 2587219.
^ Yang XM, MacKenzie RE (Nov 1993). "NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene". Biochemistry. 32 (41): 11118–23. doi:10.1021/bi00092a022. PMID 8218174.
^ "Entrez Gene: MTHFD2 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase".

Further reading※

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method——to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Kokame K, Kato H, Miyata T (1997). "Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes". J. Biol. Chem. 271 (47): 29659–65. doi:10.1074/jbc.271.47.29659. PMID 8939898.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Pawelek PD, MacKenzie RE (1998). "Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate——to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes". Biochemistry. 37 (4): 1109–15. doi:10.1021/bi971906t. PMID 9454603.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and "initial analysis of more than 15,"000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2. And 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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