CTPS1
entrez
1503
canonical
uniprot
P17812
canonical
ensembl
ENSG00000171793
resolver
ensp
ENSP00000496963
resolver
ensp
ENSP00000497602
resolver
ensp
ENSP00000497698
resolver
ensp
ENSP00000497714
resolver
ensp
ENSP00000497901
resolver
ensp
ENSP00000593317
resolver
enst
ENST00000648020
resolver
enst
ENST00000648914
resolver
enst
ENST00000649215
resolver
genesymbol
CTPS1
resolver
genesymbol_syn
CTPS
resolver
hgnc
HGNC:2519
resolver
uniprot
A0A3B3IRQ8
resolver
uniprot
A0A3B3ITB7
resolver
uniprot
A0A3B3ITB8
resolver
uniprot
B4DR64
resolver
uniprot
B4E1E0
resolver
uniprot
D3DPW1
resolver
uniprot
Q5VW67
resolver
uniprot
Q96GK6
resolver
uniprot_entry
A0A3B3IRQ8_HUMAN
resolver
uniprot_entry
A0A3B3ITB7_HUMAN
resolver
uniprot_entry
A0A3B3ITB8_HUMAN
resolver
uniprot_entry
B4E1E0_HUMAN
resolver
uniprot_entry
PYRG1_HUMAN
resolver
uniprot_sec
B4DR64
resolver
uniprot_sec
D3DPW1
resolver
uniprot_sec
Q5VW67
resolver
uniprot_sec
Q96GK6
resolver
activity_regulation
ACTIVITY REGULATION: Polymerizes into filaments upon substrate-binding, increasing the CTP synthase activity (PubMed:28459447). In contrast to CTPS2, only weakly inhibited by CTP; CTP synthase activity at higher CTP concentrations is consistent with its critical role in expanding nucleotide pools in proliferating cells (PubMed:34583994). Activated by GTP (PubMed:2113467). Specifically inhibited by small compound R80 (PubMed:34583994). {ECO:0000269|PubMed:28459447, ECO:0000269|PubMed:34583994, ECO:0000303|PubMed:2113467}.
uniprot
proteins
amino_acid_sequence
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 24 (IMD24) [MIM:615897]: A life-threatening immunodeficiency, characterized by an impaired capacity of activated T and B cells to proliferate in response to antigen receptor-mediated activation. Patients have early onset of severe chronic viral infections, mostly caused by herpes viruses, including EBV and varicella zooster virus (VZV), and also suffer from recurrent encapsulated bacterial infections, a spectrum of infections typical of a combined deficiency of adaptive immunity. {ECO:0000269|PubMed:24870241, ECO:0000269|PubMed:32161190}. Note=The disease is caused by variants affecting the gene represented in this entry. A unique and recessive G to C hypomorphic mutation affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a 80%-90% reduction of protein expression and CTP synthase activity. {ECO:0000269|PubMed:24870241, ECO:0000269|PubMed:32161190}.
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
ec_number
6.3.4.2
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P70698, ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:17189248, ECO:0000269|PubMed:17463002, ECO:0000269|PubMed:24870241, ECO:0000269|PubMed:28459447, ECO:0000269|PubMed:34583994, ECO:0000269|PubMed:40240600, ECO:0000269|PubMed:8530356}.
uniprot
proteins
mass_dalton
66690
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="T->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248, ECO:0000269|PubMed:17463002"; MUTAGEN 161; /note="E->K: Localizes to cystolic filament structures."; /evidence="ECO:0000269|PubMed:25223282"; MUTAGEN 219; /note="S->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 250; /note="I->T: Abolished inhibition by small compound R80."; /evidence="ECO:0000269|PubMed:28459447"; MUTAGEN 355; /note="H->A: Abolished ability to polymerize into filaments in presence of substrates, leading to decreased CTP synthase activity."; /evidence="ECO:0000269|PubMed:28459447"; MUTAGEN 378; /note="T->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 399; /note="C->A: Abolished protein-asparagine deamidase activity; when associated with 526-A--A-528."; /evidence="ECO:0000269|PubMed:40240600"; MUTAGEN 455; /note="T->A: Increased CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 462; /note="S->A: Decreased CTP synthase activity."; /evidence="ECO:0000269|PubMed:17463002"; MUTAGEN 526..528; /note="HPE->APA: Abolished protein-asparagine deamidase activity; when associated with A-399."; /evidence="ECO:0000269|PubMed:40240600"; MUTAGEN 552; /note="S->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 562; /note="S->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 566; /note="T->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 571; /note="S->A: Decreased phosphorylation by GSK3-beta."; /evidence="ECO:0000269|PubMed:17681942"; MUTAGEN 573; /note="S->A: Does not affect the CTP synthase activity."; /evidence="ECO:0000269|PubMed:17189248"; MUTAGEN 575; /note="S->A: Decreased phosphorylation by GSK3-beta."; /evidence="ECO:0000269|PubMed:17681942
uniprot
proteins
pathway_participation
PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241, ECO:0000269|PubMed:28459447, ECO:0000269|PubMed:34583994}.
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:P70698, ECO:0000269|PubMed:17189248, ECO:0000269|PubMed:17463002, ECO:0000269|PubMed:17681942}.
uniprot
proteins
protein_family
CTP synthase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16179339
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16820675
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17189248
uniprot
proteins
pubmed
17463002
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
17681942
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2113467
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24503052
uniprot
proteins
pubmed
24870241
uniprot
proteins
pubmed
25223282
uniprot
proteins
pubmed
28459447
uniprot
proteins
pubmed
32161190
uniprot
proteins
pubmed
34583994
uniprot
proteins
pubmed
40240600
uniprot
proteins
pubmed
8530356
uniprot
proteins
sequence_length
591
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24503052, ECO:0000269|PubMed:25223282}. Nucleus {ECO:0000269|PubMed:24503052, ECO:0000269|PubMed:40240600}. Chromosome {ECO:0000269|PubMed:40240600}. Note=Cytoplasmic and nuclear; when active, detected in long filamentous structures named cytoophidium (PubMed:24503052, PubMed:25223282, PubMed:28459447). Enriched on chromatin in response to DNA damage (PubMed:40240600). {ECO:0000269|PubMed:24503052, ECO:0000269|PubMed:25223282, ECO:0000269|PubMed:28459447, ECO:0000269|PubMed:40240600}.
uniprot
proteins