Version 5.4
Homo sapiens Protein: MTHFS
Summary
InnateDB Protein IDBP-25549.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MTHFS
Protein Name 5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000258874
InnateDB Gene IDBG-25547 (MTHFS)
Protein Structure
UniProt Annotation
Function Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10- methenyltetrahydrofolate. {ECO:0000269PubMed:8522195}.
Subcellular Localization Cytoplasm.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
Experimentally validated
Total 3 [view]
Protein-Protein 2 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005524 ATP binding
GO:0005542 folic acid binding
GO:0030272 5-formyltetrahydrofolate cyclo-ligase activity
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0015942 formate metabolic process
GO:0046653 tetrahydrofolate metabolic process
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR002698 5-formyltetrahydrofolate cyclo-ligase
PFAM PF01812
PRINTS
PIRSF PIRSF006806
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P49914
PhosphoSite PhosphoSite-P49914
TrEMBL Q96EE9
UniProt Splice Variant
Entrez Gene 10588
UniGene Hs.564779
RefSeq NP_006432
HUGO HGNC:7437
OMIM 604197
CCDS CCDS10311
HPRD 09174
IMGT
EMBL AC015871 AC021483 BC012417 BC019921 CK002935 L38928
GenPept AAC41945 AAH12417 AAH19921

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca