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Serine hydroxymethyltransferase, mitochondrial

A serine hydroxymethyltransferase, mitochondrial that is encoded in the genome of human. [PRO:DNx, UniProtKB:P34897]

Synonyms

SHMT;
EC 2.1.2.1;
Glycine hydroxymethyltransferase;
Serine methylase

Research

Bioassay Publications (0)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0)18.7374
1990's0 (0)18.2507
2000's0 (0)29.6817
2010's0 (0)24.3611
2020's0 (0)2.80

Compounds (9)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
oxaprozinHomo sapiens (human)IC501.949810
papaverineHomo sapiens (human)IC502.691510
primaquineHomo sapiens (human)IC500.436510
flupirtineHomo sapiens (human)IC500.933210
duloxetineHomo sapiens (human)IC506.918310
N-[7-(2-furanyl)-5-oxo-7,8-dihydro-6H-quinazolin-2-yl]acetamideHomo sapiens (human)IC504.570010
pyrviniumHomo sapiens (human)IC502.570410
2-(2-furanylmethyl)-3-[[2-(3-pyridinyl)-3H-benzimidazol-5-yl]amino]-3H-isoindol-1-oneHomo sapiens (human)IC509.770010
gw2974Homo sapiens (human)IC502.454710

Enables

This protein enables 7 target(s):

TargetCategoryDefinition
chromatin bindingmolecular functionBinding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. [GOC:jl, ISBN:0198506732, PMID:20404130]
glycine hydroxymethyltransferase activitymolecular functionCatalysis of the reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. [RHEA:15481]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
L-allo-threonine aldolase activitymolecular functionCatalysis of the reaction: L-allo-threonine = glycine + acetaldehyde. [PMID:9228760, RHEA:26209]
amino acid bindingmolecular functionBinding to an amino acid, organic acids containing one or more amino substituents. [GOC:ai]
pyridoxal phosphate bindingmolecular functionBinding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. [GOC:mah, ISBN:0198506732]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]

Located In

This protein is located in 8 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
mitochondrial inner membranecellular componentThe inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai]
mitochondrial matrixcellular componentThe gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732]
microtubule cytoskeletoncellular componentThe part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. [GOC:jl, ISBN:0395825172]
mitochondrial nucleoidcellular componentThe region of a mitochondrion to which the DNA is confined. [GOC:jl]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
BRISC complexcellular componentA protein complex that contains the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1 proteins, and specifically cleaves K63-linked polyubiquitin chains. [GOC:mah, PMID:19214193]

Involved In

This protein is involved in 15 target(s):

TargetCategoryDefinition
regulation of oxidative phosphorylationbiological processAny process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis. [GOC:dph]
glycine metabolic processbiological processThe chemical reactions and pathways involving glycine, aminoethanoic acid. [GOC:go_curators]
L-serine metabolic processbiological processThe chemical reactions and pathways involving L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. [GOC:ai, GOC:jsg]
L-serine biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. [GOC:ai, GOC:jsg]
one-carbon metabolic processbiological processThe chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states. [GOC:hjd, GOC:mah, GOC:pde]
positive regulation of cell population proliferationbiological processAny process that activates or increases the rate or extent of cell proliferation. [GOC:go_curators]
response to type I interferonbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. [GOC:add, ISBN:0126896631, PMID:15546383, PMID:16681834]
tetrahydrofolate interconversionbiological processThe chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules. [GOC:yaf, PMID:1825999]
tetrahydrofolate metabolic processbiological processThe chemical reactions and pathways involving tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group. [ISBN:0198506732]
protein tetramerizationbiological processThe formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits. [GOC:ecd]
protein homotetramerizationbiological processThe formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits. [GOC:go_curators]
regulation of mitochondrial translationbiological processAny process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA in a mitochondrion. [GOC:mah]
protein K63-linked deubiquitinationbiological processA protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a protein. [GOC:mah, PMID:19202061, PMID:19214193]
regulation of aerobic respirationbiological processAny process that modulates the frequency, rate or extent of aerobic respiration. [GO_REF:0000058, GOC:TermGenie, PMID:19266076]
glycine biosynthetic process from serinebiological processThe chemical reactions and pathways resulting in the formation of glycine from other compounds, including serine. [GOC:go_curators]