Full text data of CTPS2
CTPS2
[Confidence: low (only semi-automatic identification from reviews)]
CTP synthase 2; 6.3.4.2 (CTP synthetase 2; UTP--ammonia ligase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
CTP synthase 2; 6.3.4.2 (CTP synthetase 2; UTP--ammonia ligase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NRF8
ID PYRG2_HUMAN Reviewed; 586 AA.
AC Q9NRF8; B3KWM2; Q9BRI0; Q9H809; Q9H8K9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=CTP synthase 2;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 2;
DE AltName: Full=UTP--ammonia ligase 2;
GN Name=CTPS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10899599; DOI=10.1016/S0167-4781(00)00141-X;
RA van Kuilenburg A.B.P., Meinsma R., Vreken P., Waterham H.R.,
RA van Gennip A.H.;
RT "Identification of a cDNA encoding an isoform of human CTP
RT synthetase.";
RL Biochim. Biophys. Acta 1492:548-552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Retinoblastoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
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
RT reveals phosphorylation by protein kinase A.";
RL J. Biol. Chem. 280:38328-38336(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND
RP SER-574, AND MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND
RP SER-574, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-571, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC Constitutes the rate-limiting enzyme in the synthesis of cytosine
CC nucleotides.
CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC CTP + L-glutamate.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC pathway; CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; AF226667; AAF91241.1; -; mRNA.
DR EMBL; AK023549; BAB14607.1; -; mRNA.
DR EMBL; AK024070; BAB14814.1; -; mRNA.
DR EMBL; AK125332; BAG54184.1; -; mRNA.
DR EMBL; AK125348; BAG54188.1; -; mRNA.
DR EMBL; AL445467; CAI40086.1; -; Genomic_DNA.
DR EMBL; AC073909; CAI40086.1; JOINED; Genomic_DNA.
DR EMBL; CH471074; EAW98912.1; -; Genomic_DNA.
DR EMBL; BC006256; AAH06256.2; -; mRNA.
DR EMBL; BC034986; AAH34986.1; -; mRNA.
DR RefSeq; NP_001137474.1; NM_001144002.1.
DR RefSeq; NP_062831.3; NM_019857.4.
DR RefSeq; NP_787055.1; NM_175859.2.
DR RefSeq; XP_005274619.1; XM_005274562.1.
DR RefSeq; XP_005274620.1; XM_005274563.1.
DR UniGene; Hs.227049; -.
DR PDB; 2V4U; X-ray; 2.30 A; A=297-562.
DR PDB; 2VKT; X-ray; 2.50 A; A=297-562.
DR PDB; 3IHL; X-ray; 2.80 A; A/B=1-275.
DR PDBsum; 2V4U; -.
DR PDBsum; 2VKT; -.
DR PDBsum; 3IHL; -.
DR ProteinModelPortal; Q9NRF8; -.
DR SMR; Q9NRF8; 1-273, 297-562.
DR IntAct; Q9NRF8; 6.
DR MINT; MINT-1443035; -.
DR STRING; 9606.ENSP00000352222; -.
DR PhosphoSite; Q9NRF8; -.
DR DMDM; 74752919; -.
DR PaxDb; Q9NRF8; -.
DR PRIDE; Q9NRF8; -.
DR DNASU; 56474; -.
DR Ensembl; ENST00000359276; ENSP00000352222; ENSG00000047230.
DR Ensembl; ENST00000380241; ENSP00000369590; ENSG00000047230.
DR Ensembl; ENST00000443824; ENSP00000401264; ENSG00000047230.
DR GeneID; 56474; -.
DR KEGG; hsa:56474; -.
DR UCSC; uc004cxk.3; human.
DR CTD; 56474; -.
DR GeneCards; GC0XM016606; -.
DR HGNC; HGNC:2520; CTPS2.
DR HPA; HPA017437; -.
DR MIM; 300380; gene.
DR neXtProt; NX_Q9NRF8; -.
DR PharmGKB; PA27021; -.
DR eggNOG; COG0504; -.
DR HOGENOM; HOG000077514; -.
DR HOVERGEN; HBG002243; -.
DR InParanoid; Q9NRF8; -.
DR KO; K01937; -.
DR OMA; FEVNPNL; -.
DR OrthoDB; EOG7M3HZZ; -.
DR BioCyc; MetaCyc:HS00585-MONOMER; -.
DR BRENDA; 6.3.4.2; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00159; UER00277.
DR EvolutionaryTrace; Q9NRF8; -.
DR GeneWiki; CTPS2; -.
DR GenomeRNAi; 56474; -.
DR NextBio; 62001; -.
DR PRO; PR:Q9NRF8; -.
DR Bgee; Q9NRF8; -.
DR CleanEx; HS_CTPS2; -.
DR Genevestigator; Q9NRF8; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; EXP:Reactome.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; TAS:ProtInc.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1 586 CTP synthase 2.
FT /FTId=PRO_0000247033.
FT DOMAIN 300 554 Glutamine amidotransferase type-1.
FT ACT_SITE 399 399 For GATase activity (By similarity).
FT ACT_SITE 526 526 For GATase activity (By similarity).
FT ACT_SITE 528 528 For GATase activity (By similarity).
FT MOD_RES 568 568 Phosphoserine.
FT MOD_RES 571 571 Phosphoserine.
FT MOD_RES 574 574 Phosphoserine.
FT CONFLICT 220 220 T -> S (in Ref. 2; BAB14814).
FT CONFLICT 233 233 F -> L (in Ref. 2; BAB14607).
FT CONFLICT 304 304 V -> A (in Ref. 2; BAB14607).
FT STRAND 2 8
FT STRAND 10 15
FT HELIX 16 28
FT TURN 29 31
FT STRAND 34 40
FT STRAND 87 89
FT HELIX 90 102
FT TURN 103 108
FT HELIX 113 129
FT STRAND 141 147
FT HELIX 154 156
FT HELIX 157 169
FT HELIX 172 174
FT STRAND 175 182
FT TURN 187 189
FT HELIX 195 206
FT STRAND 212 220
FT HELIX 224 233
FT HELIX 238 240
FT STRAND 241 245
FT HELIX 252 259
FT HELIX 262 270
FT STRAND 297 306
FT HELIX 312 314
FT HELIX 315 327
FT STRAND 330 338
FT HELIX 339 342
FT HELIX 344 349
FT HELIX 351 363
FT STRAND 365 369
FT HELIX 378 390
FT STRAND 395 398
FT HELIX 400 413
FT STRAND 419 422
FT STRAND 429 435
FT STRAND 449 458
FT HELIX 463 467
FT STRAND 472 480
FT STRAND 482 484
FT HELIX 486 488
FT HELIX 490 492
FT STRAND 495 503
FT STRAND 508 518
FT STRAND 520 526
FT HELIX 527 530
FT HELIX 538 548
FT HELIX 551 556
SQ SEQUENCE 586 AA; 65678 MW; AC1CF2E67D89741B CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
VQEWVMNQAK VPVDGNKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
SLVPQLSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSST YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED PVKFHEAWQK
LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL GMQLAVIEFA RNCLNLKDAD
STEFRPNAPV PLVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH
RFEVNPNLIK QFEQNDLSFV GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY
LGLLLAATGN LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS
//
ID PYRG2_HUMAN Reviewed; 586 AA.
AC Q9NRF8; B3KWM2; Q9BRI0; Q9H809; Q9H8K9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=CTP synthase 2;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 2;
DE AltName: Full=UTP--ammonia ligase 2;
GN Name=CTPS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10899599; DOI=10.1016/S0167-4781(00)00141-X;
RA van Kuilenburg A.B.P., Meinsma R., Vreken P., Waterham H.R.,
RA van Gennip A.H.;
RT "Identification of a cDNA encoding an isoform of human CTP
RT synthetase.";
RL Biochim. Biophys. Acta 1492:548-552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Retinoblastoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
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
RT reveals phosphorylation by protein kinase A.";
RL J. Biol. Chem. 280:38328-38336(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND
RP SER-574, AND MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND
RP SER-574, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-571, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC Constitutes the rate-limiting enzyme in the synthesis of cytosine
CC nucleotides.
CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CC CTP + L-glutamate.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC pathway; CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; AF226667; AAF91241.1; -; mRNA.
DR EMBL; AK023549; BAB14607.1; -; mRNA.
DR EMBL; AK024070; BAB14814.1; -; mRNA.
DR EMBL; AK125332; BAG54184.1; -; mRNA.
DR EMBL; AK125348; BAG54188.1; -; mRNA.
DR EMBL; AL445467; CAI40086.1; -; Genomic_DNA.
DR EMBL; AC073909; CAI40086.1; JOINED; Genomic_DNA.
DR EMBL; CH471074; EAW98912.1; -; Genomic_DNA.
DR EMBL; BC006256; AAH06256.2; -; mRNA.
DR EMBL; BC034986; AAH34986.1; -; mRNA.
DR RefSeq; NP_001137474.1; NM_001144002.1.
DR RefSeq; NP_062831.3; NM_019857.4.
DR RefSeq; NP_787055.1; NM_175859.2.
DR RefSeq; XP_005274619.1; XM_005274562.1.
DR RefSeq; XP_005274620.1; XM_005274563.1.
DR UniGene; Hs.227049; -.
DR PDB; 2V4U; X-ray; 2.30 A; A=297-562.
DR PDB; 2VKT; X-ray; 2.50 A; A=297-562.
DR PDB; 3IHL; X-ray; 2.80 A; A/B=1-275.
DR PDBsum; 2V4U; -.
DR PDBsum; 2VKT; -.
DR PDBsum; 3IHL; -.
DR ProteinModelPortal; Q9NRF8; -.
DR SMR; Q9NRF8; 1-273, 297-562.
DR IntAct; Q9NRF8; 6.
DR MINT; MINT-1443035; -.
DR STRING; 9606.ENSP00000352222; -.
DR PhosphoSite; Q9NRF8; -.
DR DMDM; 74752919; -.
DR PaxDb; Q9NRF8; -.
DR PRIDE; Q9NRF8; -.
DR DNASU; 56474; -.
DR Ensembl; ENST00000359276; ENSP00000352222; ENSG00000047230.
DR Ensembl; ENST00000380241; ENSP00000369590; ENSG00000047230.
DR Ensembl; ENST00000443824; ENSP00000401264; ENSG00000047230.
DR GeneID; 56474; -.
DR KEGG; hsa:56474; -.
DR UCSC; uc004cxk.3; human.
DR CTD; 56474; -.
DR GeneCards; GC0XM016606; -.
DR HGNC; HGNC:2520; CTPS2.
DR HPA; HPA017437; -.
DR MIM; 300380; gene.
DR neXtProt; NX_Q9NRF8; -.
DR PharmGKB; PA27021; -.
DR eggNOG; COG0504; -.
DR HOGENOM; HOG000077514; -.
DR HOVERGEN; HBG002243; -.
DR InParanoid; Q9NRF8; -.
DR KO; K01937; -.
DR OMA; FEVNPNL; -.
DR OrthoDB; EOG7M3HZZ; -.
DR BioCyc; MetaCyc:HS00585-MONOMER; -.
DR BRENDA; 6.3.4.2; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00159; UER00277.
DR EvolutionaryTrace; Q9NRF8; -.
DR GeneWiki; CTPS2; -.
DR GenomeRNAi; 56474; -.
DR NextBio; 62001; -.
DR PRO; PR:Q9NRF8; -.
DR Bgee; Q9NRF8; -.
DR CleanEx; HS_CTPS2; -.
DR Genevestigator; Q9NRF8; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; EXP:Reactome.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; TAS:ProtInc.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1 586 CTP synthase 2.
FT /FTId=PRO_0000247033.
FT DOMAIN 300 554 Glutamine amidotransferase type-1.
FT ACT_SITE 399 399 For GATase activity (By similarity).
FT ACT_SITE 526 526 For GATase activity (By similarity).
FT ACT_SITE 528 528 For GATase activity (By similarity).
FT MOD_RES 568 568 Phosphoserine.
FT MOD_RES 571 571 Phosphoserine.
FT MOD_RES 574 574 Phosphoserine.
FT CONFLICT 220 220 T -> S (in Ref. 2; BAB14814).
FT CONFLICT 233 233 F -> L (in Ref. 2; BAB14607).
FT CONFLICT 304 304 V -> A (in Ref. 2; BAB14607).
FT STRAND 2 8
FT STRAND 10 15
FT HELIX 16 28
FT TURN 29 31
FT STRAND 34 40
FT STRAND 87 89
FT HELIX 90 102
FT TURN 103 108
FT HELIX 113 129
FT STRAND 141 147
FT HELIX 154 156
FT HELIX 157 169
FT HELIX 172 174
FT STRAND 175 182
FT TURN 187 189
FT HELIX 195 206
FT STRAND 212 220
FT HELIX 224 233
FT HELIX 238 240
FT STRAND 241 245
FT HELIX 252 259
FT HELIX 262 270
FT STRAND 297 306
FT HELIX 312 314
FT HELIX 315 327
FT STRAND 330 338
FT HELIX 339 342
FT HELIX 344 349
FT HELIX 351 363
FT STRAND 365 369
FT HELIX 378 390
FT STRAND 395 398
FT HELIX 400 413
FT STRAND 419 422
FT STRAND 429 435
FT STRAND 449 458
FT HELIX 463 467
FT STRAND 472 480
FT STRAND 482 484
FT HELIX 486 488
FT HELIX 490 492
FT STRAND 495 503
FT STRAND 508 518
FT STRAND 520 526
FT HELIX 527 530
FT HELIX 538 548
FT HELIX 551 556
SQ SEQUENCE 586 AA; 65678 MW; AC1CF2E67D89741B CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
VQEWVMNQAK VPVDGNKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
SLVPQLSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSST YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED PVKFHEAWQK
LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL GMQLAVIEFA RNCLNLKDAD
STEFRPNAPV PLVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH
RFEVNPNLIK QFEQNDLSFV GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY
LGLLLAATGN LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS
//
MIM
300380
*RECORD*
*FIELD* NO
300380
*FIELD* TI
*300380 CYTIDINE 5-PRIME TRIPHOSPHATE SYNTHETASE 2; CTPS2
;;CTP SYNTHETASE 2;;
CTP SYNTHASE 2
read more*FIELD* TX
DESCRIPTION
CTP synthetase (EC 6.3.4.2) catalyzes the formation of CTP from UTP with
the concomitant deamination of glutamine to glutamate. CTP synthetase is
the rate-limiting enzyme in the synthesis of cytosine nucleotides, which
play an important role in various metabolic processes and provide the
precursors necessary for the synthesis of RNA and DNA. Cancer cells that
exhibit increased cell proliferation also exhibit an increased activity
of CTP synthetase. Thus, CTP synthetase is an attractive target for
selective chemotherapy (van Kuilenburg et al., 2000).
CLONING
Van Kuilenburg et al. (2000) screened an EST database with the CTPS
(123860) sequence and identified CTPS2. Using PCR and RACE with liver
cDNA, they cloned a full-length CTPS2 cDNA predicted to encode a
586-amino acid protein that shares 74% amino acid identity with CTPS.
GENE FUNCTION
Van Kuilenburg et al. (2000) demonstrated that CTPS2 can function as a
CTP synthetase by successfully complementing the phenotype of a
cytidine-requiring CTP synthetase-deficient mutant in E. coli.
MAPPING
By genomic sequence analysis, van Kuilenburg et al. (2000) mapped the
CTPS2 gene to chromosome Xp22.
*FIELD* RF
1. van Kuilenburg, A. B. P.; Meinsma, R.; Vreken, P.; Waterham, H.
R.; van Gennip, A. H.: Identification of a cDNA encoding an isoform
of human CTP synthetase. Biochim. Biophys. Acta 1492: 548-552, 2000.
*FIELD* CD
Dawn Watkins-Chow: 2/26/2002
*FIELD* ED
mgross: 02/26/2002
*RECORD*
*FIELD* NO
300380
*FIELD* TI
*300380 CYTIDINE 5-PRIME TRIPHOSPHATE SYNTHETASE 2; CTPS2
;;CTP SYNTHETASE 2;;
CTP SYNTHASE 2
read more*FIELD* TX
DESCRIPTION
CTP synthetase (EC 6.3.4.2) catalyzes the formation of CTP from UTP with
the concomitant deamination of glutamine to glutamate. CTP synthetase is
the rate-limiting enzyme in the synthesis of cytosine nucleotides, which
play an important role in various metabolic processes and provide the
precursors necessary for the synthesis of RNA and DNA. Cancer cells that
exhibit increased cell proliferation also exhibit an increased activity
of CTP synthetase. Thus, CTP synthetase is an attractive target for
selective chemotherapy (van Kuilenburg et al., 2000).
CLONING
Van Kuilenburg et al. (2000) screened an EST database with the CTPS
(123860) sequence and identified CTPS2. Using PCR and RACE with liver
cDNA, they cloned a full-length CTPS2 cDNA predicted to encode a
586-amino acid protein that shares 74% amino acid identity with CTPS.
GENE FUNCTION
Van Kuilenburg et al. (2000) demonstrated that CTPS2 can function as a
CTP synthetase by successfully complementing the phenotype of a
cytidine-requiring CTP synthetase-deficient mutant in E. coli.
MAPPING
By genomic sequence analysis, van Kuilenburg et al. (2000) mapped the
CTPS2 gene to chromosome Xp22.
*FIELD* RF
1. van Kuilenburg, A. B. P.; Meinsma, R.; Vreken, P.; Waterham, H.
R.; van Gennip, A. H.: Identification of a cDNA encoding an isoform
of human CTP synthetase. Biochim. Biophys. Acta 1492: 548-552, 2000.
*FIELD* CD
Dawn Watkins-Chow: 2/26/2002
*FIELD* ED
mgross: 02/26/2002