Overview
| Uniprot ID | P17812 |
|---|
| Protein Name | CTP synthase 1 |
|---|
| Gene Name | CTPS1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 100 |
IYQYVINKERKGDYL |
| 309 |
ALVGKYTKFSDSYAS |
| 466 |
TKNSVMRKLYGDADY |
| 489 |
FEVNPVWKKCLEEQG |
| 490 |
EVNPVWKKCLEEQGL |
| 557 |
RLSHYLQKGCRLSPR |
| 84 |
FLDIRLTKDNNLTTG |
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)
Protein Sequence
10
MKYILVTGGV
20
ISGIGKGIIA
30
SSVGTILKSC
40
GLHVTSIKID
50
PYINIDAGTF
60
SPYEHGEVFV
70
LDDGGEVDLD
80
LGNYERFLDI
90
RLTKDNNLTT
100
GKIYQYVINK
110
ERKGDYLGKT
120
VQVVPHITDA
130
IQEWVMRQAL
140
IPVDEDGLEP
150
QVCVIELGGT
160
VGDIESMPFI
170
EAFRQFQFKV
180
KRENFCNIHV
190
SLVPQPSSTG
200
EQKTKPTQNS
210
VRELRGLGLS
220
PDLVVCRCSN
230
PLDTSVKEKI
240
SMFCHVEPEQ
250
VICVHDVSSI
260
YRVPLLLEEQ
270
GVVDYFLRRL
280
DLPIERQPRK
290
MLMKWKEMAD
300
RYDRLLETCS
310
IALVGKYTKF
320
SDSYASVIKA
330
LEHSALAINH
340
KLEIKYIDSA
350
DLEPITSQEE
360
PVRYHEAWQK
370
LCSAHGVLVP
380
GGFGVRGTEG
390
KIQAIAWARN
400
QKKPFLGVCL
410
GMQLAVVEFS
420
RNVLGWQDAN
430
STEFDPTTSH
440
PVVVDMPEHN
450
PGQMGGTMRL
460
GKRRTLFQTK
470
NSVMRKLYGD
480
ADYLEERHRH
490
RFEVNPVWKK
500
CLEEQGLKFV
510
GQDVEGERME
520
IVELEDHPFF
530
VGVQYHPEFL
540
SRPIKPSPPY
550
FGLLLASVGR
560
LSHYLQKGCR
570
LSPRDTYSDR
580
SGSSSPDSEI
590
TELKFPSINH
D
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0097268 |
cytoophidium |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0003883 |
CTP synthase activity |
| Molecular Function |
GO:0160264 |
histone H1N76/N77 asparagine deamidase activity |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0160260 |
protein asparagine deamidase activity |
| Biological Process |
GO:0044210 |
'de novo' CTP biosynthetic process |
| Biological Process |
GO:0042100 |
B cell proliferation |
| Biological Process |
GO:0006241 |
CTP biosynthetic process |
| Biological Process |
GO:0140861 |
DNA repair-dependent chromatin remodeling |
| Biological Process |
GO:1902340 |
negative regulation of chromosome condensation |
| Biological Process |
GO:0032480 |
negative regulation of type I interferon production |
| Biological Process |
GO:0006139 |
nucleobase-containing compound metabolic process |
| Biological Process |
GO:0019856 |
pyrimidine nucleobase biosynthetic process |
| Biological Process |
GO:0009410 |
response to xenobiotic stimulus |
| Biological Process |
GO:0042098 |
T cell proliferation |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.