Recombinant Human CTP synthase/CTPS protein (GST tag N-Terminus)
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Recombinant Human CTP synthase/CTPS protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 591 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
CTPS, CTPS1, CTP synthase 1, CTP synthetase 1, Protein-asparagine deamidase CTPS1, UTP--ammonia ligase 1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human CTP synthase/CTPS protein (GST tag N-Terminus) (AB132558)
12.5% SDS-PAGE analysis of ab132558 stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CTP synthase plays a significant role in the regulation of nucleotide pools. The enzyme ensures the balance of CTP levels necessary for DNA RNA and phospholipid synthesis acting as a rate-limiting step in these processes. CTPS is part of larger enzymatic complexes that aid in cellular response to nutrient availability and DNA damage. Allosteric regulation and product feedback inhibition modulate CTP synthase activity maintaining cellular homeostasis and a proper supply of CTP for various biosynthetic pathways.
Pathways
CTP synthase is an important component in the pyrimidine biosynthesis pathway essential for nucleic acid and lipid metabolism. The enzyme's activity is tightly linked to the salvage pathways collaborating with enzymes like ribonucleotide reductase to regulate deoxyribonucleotide levels for DNA replication and repair. These interactions highlight the enzyme's involvement in cellular proliferation and response to metabolic stresses underpinning its regulatory function in metabolic pathways.
Specifications
Form
Liquid
General info
Function
CTP synthase involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids (PubMed : 16179339, PubMed : 17189248, PubMed : 17463002, PubMed : 24870241, PubMed : 28459447, PubMed : 34583994). Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen (PubMed : 16179339, PubMed : 24870241, PubMed : 28459447, PubMed : 34583994). CTPS1 CTP synthase activity plays a crucial role in the proliferation of activated lymphocytes and immunity; additional CTP being required to meet increased demand for DNA, RNA and lipid membrane biosynthesis in proliferating lymphocytes (PubMed : 24870241, PubMed : 8530356). In addition to CTP synthase activity, also acts as a protein deamidase that catalyzes the side chain deamidation of specific asparagine residues of proteins to aspartate (PubMed : 40240600). Acts as a negative regulator of innate immunity by mediating deamidation of 'Asn-85' of IRF3, preventing IRF3 from binding DNA (By similarity). Facilitates chromatin relaxation in response to DNA damage by mediating deamidation of 'Asn-76' and 'Asn-77' of histone H1, thereby promoting subsequent acetylation of histone H1 at 'Lys-75' (H1K75ac), increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins (PubMed : 40240600).
Sequence similarities
Belongs to the CTP synthase family.
Post-translational modifications
Phosphorylation at Thr-455 by PKA and PKC inhibits the CTP synthase activity (PubMed:17189248, PubMed:17463002). Phosphorylation at Ser-462 by PKC increases the CTP synthase activity (PubMed:17463002). Phosphorylation by GSK3-beta (GSK3B) inhibits both the CTP synthase and protein deamidase activities (PubMed:17681942). Phosphorylation at Ser-571 by GSK3-beta (GSK3B) constitutes the major phosphorylation site, while phosphorylation at Ser-575 may by required for priming phosphorylation at Ser-571 (PubMed:17681942). Phosphorylation at Ser-575 by GSK3-beta (GSK3B) inhibits its ability to mediate deamination of IRF3 (By similarity).
Subcellular localisation
Nucleus
Target data
Product promise
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