ID PYRG1_HUMAN Reviewed; 591 AA. AC P17812; B4DR64; D3DPW1; Q5VW67; Q96GK6; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=CTP synthase 1 {ECO:0000305}; DE EC=6.3.4.2 {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}; DE AltName: Full=CTP synthetase 1; DE AltName: Full=UTP--ammonia ligase 1; GN Name=CTPS1 {ECO:0000312|HGNC:HGNC:2519}; GN Synonyms=CTPS {ECO:0000312|HGNC:HGNC:2519}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=2113467; DOI=10.1002/j.1460-2075.1990.tb07377.x; RA Yamauchi M., Yamauchi N., Meuth M.; RT "Molecular cloning of the human CTP synthetase gene by functional RT complementation with purified human metaphase chromosomes."; RL EMBO J. 9:2095-2099(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-571. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=16179339; DOI=10.1074/jbc.m509622200; RA Han G.-S., Sreenivas A., Choi M.-G., Chang Y.-F., Martin S.S., RA Baldwin E.P., Carman G.M.; RT "Expression of human CTP synthetase in Saccharomyces cerevisiae reveals RT phosphorylation by protein kinase A."; RL J. Biol. Chem. 280:38328-38336(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573; RP SER-574; SER-575 AND SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-574 AND SER-575, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574 AND SER-575, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562; SER-573 AND SER-575, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, INDUCTION, AND RP INVOLVEMENT IN IMD24. RX PubMed=24870241; DOI=10.1038/nature13386; RA Martin E., Palmic N., Sanquer S., Lenoir C., Hauck F., Mongellaz C., RA Fabrega S., Nitschke P., Esposti M.D., Schwartzentruber J., Taylor N., RA Majewski J., Jabado N., Wynn R.F., Picard C., Fischer A., Arkwright P.D., RA Latour S.; RT "CTP synthase 1 deficiency in humans reveals its central role in lymphocyte RT proliferation."; RL Nature 510:288-292(2014). RN [22] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-161. RX PubMed=25223282; DOI=10.15252/embr.201438688; RA Strochlic T.I., Stavrides K.P., Thomas S.V., Nicolas E., O'Reilly A.M., RA Peterson J.R.; RT "Ack kinase regulates CTP synthase filaments during Drosophila oogenesis."; RL EMBO Rep. 15:1184-1191(2014). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-272. RX PubMed=16820675; DOI=10.1107/s1744309106018136; RA Kursula P., Flodin S., Ehn M., Hammarstrom M., Schuler H., Nordlund P., RA Stenmark P.; RT "Structure of the synthetase domain of human CTP synthetase, a target for RT anticancer therapy."; RL Acta Crystallogr. F 62:613-617(2006). CC -!- FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a CC precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent CC amination of UTP to CTP with either L-glutamine or ammonia as a source CC of nitrogen. This enzyme and its product, CTP, play a crucial role in CC the proliferation of activated lymphocytes and therefore in immunity. CC {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L- CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; CC Evidence={ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}; CC -!- ACTIVITY REGULATION: Activated by GTP and inhibited by CTP. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC CTP from UDP: step 2/2. {ECO:0000269|PubMed:16179339, CC ECO:0000269|PubMed:24870241}. CC -!- INTERACTION: CC P17812; P17812: CTPS1; NbExp=4; IntAct=EBI-1042983, EBI-1042983; CC P17812; Q9NRF8: CTPS2; NbExp=4; IntAct=EBI-1042983, EBI-740874; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25223282}. CC Note=Mainly cytosolic but when active detected in long filamentous CC structures (PubMed:25223282). Co-localizes with TNK2 in the cytosolic CC filaments (By similarity). {ECO:0000250|UniProtKB:P70698, CC ECO:0000269|PubMed:25223282}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P17812-1; Sequence=Displayed; CC Name=2; CC IsoId=P17812-2; Sequence=VSP_055827; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24870241}. CC -!- INDUCTION: Up-regulated in T-cells and B-cells activated through the CC TCR and the BCR respectively (at protein level). CC {ECO:0000269|PubMed:24870241}. CC -!- DISEASE: Immunodeficiency 24 (IMD24) [MIM:615897]: A life-threatening CC immunodeficiency, characterized by an impaired capacity of activated T CC and B cells to proliferate in response to antigen receptor-mediated CC activation. Patients have early onset of severe chronic viral CC infections, mostly caused by herpes viruses, including EBV and CC varicella zooster virus (VZV), and also suffer from recurrent CC encapsulated bacterial infections, a spectrum of infections typical of CC a combined deficiency of adaptive immunity. CC {ECO:0000269|PubMed:24870241}. Note=The disease is caused by variants CC affecting the gene represented in this entry. A unique and recessive G CC to C mutation probably affecting a splice donor site at the junction of CC intron 17-18 and exon 18 has been identified in all patients. It CC results in expression of an abnormal transcript lacking exon 18 and a CC complete loss of the expression of the protein. CC {ECO:0000269|PubMed:24870241}. CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52142; CAA36386.1; -; mRNA. DR EMBL; AK299122; BAG61176.1; -; mRNA. DR EMBL; AL391730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07192.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07193.1; -; Genomic_DNA. DR EMBL; BC009408; AAH09408.1; -; mRNA. DR CCDS; CCDS459.1; -. [P17812-1] DR PIR; S12791; SYHUTP. DR RefSeq; NP_001288166.1; NM_001301237.1. DR RefSeq; NP_001896.2; NM_001905.3. [P17812-1] DR PDB; 2VO1; X-ray; 2.80 A; A/B=1-273. DR PDB; 5U03; EM; 6.10 A; A/B/C/D=1-591. DR PDB; 7MGZ; EM; 2.80 A; F/O/P/Q=1-591. DR PDB; 7MH0; EM; 6.20 A; A/B/C/D=1-591. DR PDB; 7MIF; EM; 3.10 A; C/G/H/I=1-591. DR PDB; 7MIG; EM; 2.90 A; A/B/C/E=1-591. DR PDBsum; 2VO1; -. DR PDBsum; 5U03; -. DR PDBsum; 7MGZ; -. DR PDBsum; 7MH0; -. DR PDBsum; 7MIF; -. DR PDBsum; 7MIG; -. DR AlphaFoldDB; P17812; -. DR EMDB; EMD-23831; -. DR EMDB; EMD-23832; -. DR EMDB; EMD-23848; -. DR EMDB; EMD-23850; -. DR EMDB; EMD-8474; -. DR EMDB; EMD-8476; -. DR SMR; P17812; -. DR BioGRID; 107883; 172. DR IntAct; P17812; 42. DR MINT; P17812; -. DR STRING; 9606.ENSP00000497744; -. DR DrugBank; DB00130; L-Glutamine. DR GuidetoPHARMACOLOGY; 3215; -. DR MEROPS; C26.A36; -. DR GlyConnect; 2032; 1 N-Linked glycan (1 site). DR GlyCosmos; P17812; 1 site, 2 glycans. DR GlyGen; P17812; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P17812; -. DR PhosphoSitePlus; P17812; -. DR SwissPalm; P17812; -. DR BioMuta; CTPS1; -. DR DMDM; 20981706; -. DR EPD; P17812; -. DR jPOST; P17812; -. DR MassIVE; P17812; -. DR MaxQB; P17812; -. DR PaxDb; 9606-ENSP00000361704; -. DR PeptideAtlas; P17812; -. DR ProteomicsDB; 4927; -. DR ProteomicsDB; 53516; -. [P17812-1] DR Pumba; P17812; -. DR Antibodypedia; 4476; 230 antibodies from 32 providers. DR DNASU; 1503; -. DR Ensembl; ENST00000372616.1; ENSP00000361699.1; ENSG00000171793.17. [P17812-1] DR Ensembl; ENST00000470271.6; ENSP00000497901.2; ENSG00000171793.17. [P17812-1] DR Ensembl; ENST00000649124.2; ENSP00000497744.1; ENSG00000171793.17. [P17812-1] DR Ensembl; ENST00000650070.2; ENSP00000497602.1; ENSG00000171793.17. [P17812-1] DR Ensembl; ENST00000696070.1; ENSP00000512372.1; ENSG00000171793.17. [P17812-2] DR GeneID; 1503; -. DR KEGG; hsa:1503; -. DR MANE-Select; ENST00000650070.2; ENSP00000497602.1; NM_001905.4; NP_001896.2. DR UCSC; uc001cgk.5; human. [P17812-1] DR AGR; HGNC:2519; -. DR CTD; 1503; -. DR DisGeNET; 1503; -. DR GeneCards; CTPS1; -. DR HGNC; HGNC:2519; CTPS1. DR HPA; ENSG00000171793; Low tissue specificity. DR MalaCards; CTPS1; -. DR MIM; 123860; gene. DR MIM; 615897; phenotype. DR neXtProt; NX_P17812; -. DR OpenTargets; ENSG00000171793; -. DR Orphanet; 420573; Severe combined immunodeficiency due to CTPS1 deficiency. DR PharmGKB; PA27020; -. DR VEuPathDB; HostDB:ENSG00000171793; -. DR eggNOG; KOG2387; Eukaryota. DR GeneTree; ENSGT00910000144179; -. DR HOGENOM; CLU_011675_5_0_1; -. DR InParanoid; P17812; -. DR OMA; EFNNAYR; -. DR OrthoDB; 166427at2759; -. DR PhylomeDB; P17812; -. DR TreeFam; TF300379; -. DR BioCyc; MetaCyc:HS10382-MONOMER; -. DR PathwayCommons; P17812; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR SignaLink; P17812; -. DR SIGNOR; P17812; -. DR UniPathway; UPA00159; UER00277. DR BioGRID-ORCS; 1503; 429 hits in 1163 CRISPR screens. DR ChiTaRS; CTPS1; human. DR EvolutionaryTrace; P17812; -. DR GeneWiki; CTP_synthase_1; -. DR GenomeRNAi; 1503; -. DR Pharos; P17812; Tbio. DR PRO; PR:P17812; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P17812; Protein. DR Bgee; ENSG00000171793; Expressed in parotid gland and 155 other cell types or tissues. DR ExpressionAtlas; P17812; baseline and differential. DR GO; GO:0097268; C:cytoophidium; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB. DR GO; GO:0006241; P:CTP biosynthetic process; IDA:UniProtKB. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0009410; P:response to xenobiotic stimulus; TAS:ProtInc. DR GO; GO:0042098; P:T cell proliferation; IMP:UniProtKB. DR CDD; cd03113; CTPS_N; 1. DR CDD; cd01746; GATase1_CTP_Synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR033828; GATase1_CTP_Synthase. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00337; PyrG; 1. DR PANTHER; PTHR11550; CTP SYNTHASE; 1. DR PANTHER; PTHR11550:SF8; CTP SYNTHASE 1; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR Genevisible; P17812; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Glutamine amidotransferase; Immunity; Ligase; Nucleotide-binding; KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..591 FT /note="CTP synthase 1" FT /id="PRO_0000138275" FT DOMAIN 300..554 FT /note="Glutamine amidotransferase type-1" FT REGION 562..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 566..582 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 399 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 526 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 528 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT MOD_RES 100 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 562 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 568 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 571 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 573 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 574 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 575 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 578 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70698" FT MOD_RES 587 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..231 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055827" FT VARIANT 571 FT /note="S -> I (in dbSNP:rs17856308)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027055" FT MUTAGEN 161 FT /note="E->K: Localizes to cystolic filament structures." FT /evidence="ECO:0000269|PubMed:25223282" FT CONFLICT 305 FT /note="G -> A (in Ref. 1; CAA36386)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="K -> E (in Ref. 1; CAA36386)" FT /evidence="ECO:0000305" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 70..78 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 90..102 FT /evidence="ECO:0007829|PDB:2VO1" FT TURN 103..108 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 113..130 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 157..169 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 175..182 FT /evidence="ECO:0007829|PDB:2VO1" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:2VO1" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 253..259 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 262..270 FT /evidence="ECO:0007829|PDB:2VO1" FT HELIX 282..294 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 297..307 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 311..314 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 315..327 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 331..338 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 351..363 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 365..369 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 378..390 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 400..412 FT /evidence="ECO:0007829|PDB:7MGZ" FT TURN 422..424 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 429..435 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 451..458 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 463..467 FT /evidence="ECO:0007829|PDB:7MGZ" FT TURN 468..470 FT /evidence="ECO:0007829|PDB:7MIG" FT STRAND 472..478 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:7MGZ" FT TURN 486..488 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 489..493 FT /evidence="ECO:0007829|PDB:7MGZ" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 497..503 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 508..514 FT /evidence="ECO:0007829|PDB:7MGZ" FT STRAND 517..525 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 527..530 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 538..547 FT /evidence="ECO:0007829|PDB:7MGZ" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:7MGZ" FT HELIX 551..554 FT /evidence="ECO:0007829|PDB:7MGZ" SQ SEQUENCE 591 AA; 66690 MW; 0B04F9D9390C4152 CRC64; MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK ERKGDYLGKT VQVVPHITDA IQEWVMRQAL IPVDEDGLEP QVCVIELGGT VGDIESMPFI EAFRQFQFKV KRENFCNIHV SLVPQPSSTG EQKTKPTQNS VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ VICVHDVSSI YRVPLLLEEQ GVVDYFLRRL DLPIERQPRK MLMKWKEMAD RYDRLLETCS IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDSA DLEPITSQEE PVRYHEAWQK LCSAHGVLVP GGFGVRGTEG KIQAIAWARN QKKPFLGVCL GMQLAVVEFS RNVLGWQDAN STEFDPTTSH PVVVDMPEHN PGQMGGTMRL GKRRTLFQTK NSVMRKLYGD ADYLEERHRH RFEVNPVWKK CLEEQGLKFV GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY FGLLLASVGR LSHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSINH D //