PYRG1_HUMAN
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 03-AUG-2022, entry version 222.
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}.
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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 SMR; P17812; -.
DR BioGRID; 107883; 119.
DR IntAct; P17812; 41.
DR MINT; P17812; -.
DR STRING; 9606.ENSP00000361704; -.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C26.A36; -.
DR GlyConnect; 2032; 1 N-Linked glycan (1 site).
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; P17812; -.
DR PeptideAtlas; P17812; -.
DR PRIDE; P17812; -.
DR ProteomicsDB; 4927; -.
DR ProteomicsDB; 53516; -. [P17812-1]
DR Antibodypedia; 4476; 181 antibodies from 32 providers.
DR DNASU; 1503; -.
DR Ensembl; ENST00000372616.1; ENSP00000361699.1; ENSG00000171793.16. [P17812-1]
DR Ensembl; ENST00000649124.1; ENSP00000497744.1; ENSG00000171793.16. [P17812-1]
DR Ensembl; ENST00000650070.2; ENSP00000497602.1; ENSG00000171793.16. [P17812-1]
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 CTD; 1503; -.
DR DisGeNET; 1503; -.
DR GeneCards; CTPS1; -.
DR HGNC; HGNC:2519; CTPS1.
DR HPA; ENSG00000171793; Tissue enhanced (liver).
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; 810128at2759; -.
DR PhylomeDB; P17812; -.
DR TreeFam; TF300379; -.
DR BioCyc; MetaCyc:HS10382-MON; -.
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; 398 hits in 1081 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 153 other tissues.
DR ExpressionAtlas; P17812; baseline and differential.
DR Genevisible; P17812; HS.
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; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
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
