Search by BoMiProt ID - Bomi288

Primary Information

BoMiProt ID Bomi288
Protein Name Serine hydroxymethyltransferase, cytosolic
Organism Bos taurus
Uniprot IDQ5E9P9
Milk FractionWhey
Ref Sequence ID NP_001015553.1
Aminoacid Length 484
Molecular Weight 52978
FASTA Sequence Download
Gene Name SHMT1
Gene ID 509002
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function Catalyzes the reversible conversion of L-serine and tetrahydrofolate into glycine and 5,10-methylenetetrahydrofolate; plays a pivotal role in one-carbon metabolism; is involved in cancer metabolic reprogramming and is a recognized target of chemotherapy intervention
Biochemical Properties pH optimum of SHMT mitochondrial is 0.5 unit higher with respect to that of SHMTcytosolic; cytosolic SHMT shows a marked decrease in the level of substrate inhibition at high pH values; in the case of SHMT1, below 20 μM Tetrahydrofolate, the enzyme activity decreases as the pH is increased from 6.9 to 8.4
Significance in milk May be related to stage-specific expression, varying throughout gestation and rising after birth as found in swines
PTMs Ubiquitinated at the small ubiquitin-like modifier (SUMO) consensus motif ; SUMO-1 modification occurs at either Lys-38 or Lys-39
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs As found in vivo, ubiquitinationis required for SHMT1 degradation; SUMOylation is required for nuclear transport
Bibliography 1. Vallée, M. et al. (2002) ‘Effects of Breed, Parity, and Folic Acid Supplement on the Expression of Folate Metabolism Genes in Endometrial and Embryonic Tissues from Sows in Early Pregnancy1’, Biology of Reproduction, 67(4), pp. 1259–1267. doi: 10.1095/biolreprod67.4.1259.
2. Anderson, D. D., Eom, J. Y. and Stover, P. J. (2012) ‘Competition between Sumoylation and Ubiquitination of Serine Hydroxymethyltransferase 1 Determines Its Nuclear Localization and Its Accumulation in the Nucleus’, Journal of Biological Chemistry, 287(7), pp. 4790–4799. doi: 10.1074/jbc.M111.302174.
3. Tramonti, A. et al. (2018) ‘Human Cytosolic and Mitochondrial Serine Hydroxymethyltransferase Isoforms in Comparison: Full Kinetic Characterization and Substrate Inhibition Properties.’, Biochemistry, 57(51), pp. 6984–6996. doi: 10.1021/acs.biochem.8b01074.