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P17812 (PYRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CTP synthase 1

EC=6.3.4.2
Alternative name(s):
CTP synthetase 1
UTP--ammonia ligase 1
Gene names
Name:CTPS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Ref.6

Catalytic activity

ATP + UTP + NH3 = ADP + phosphate + CTP.

Enzyme regulation

Activated by GTP and inhibited by CTP.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.

Sequence similarities

Belongs to the CTP synthase family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591CTP synthase 1
PRO_0000138275

Regions

Domain300 – 554255Glutamine amidotransferase type-1

Sites

Active site3991For GATase activity By similarity
Active site5261For GATase activity By similarity
Active site5281For GATase activity By similarity

Amino acid modifications

Modified residue1001N6-acetyllysine Ref.17
Modified residue5621Phosphoserine Ref.9
Modified residue5661Phosphothreonine By similarity
Modified residue5671Phosphotyrosine By similarity
Modified residue5681Phosphoserine Ref.10 Ref.13 Ref.14
Modified residue5711Phosphoserine Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16
Modified residue5731Phosphoserine Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15
Modified residue5741Phosphoserine Ref.8 Ref.10 Ref.13 Ref.14 Ref.16
Modified residue5751Phosphoserine Ref.5 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
Modified residue5811Phosphothreonine Ref.13
Modified residue5871Phosphoserine Ref.13

Natural variations

Natural variant5711S → I. Ref.4
Corresponds to variant rs17856308 [ dbSNP | Ensembl ].
VAR_027055

Experimental info

Sequence conflict3051G → A in CAA36386. Ref.1
Sequence conflict3091K → E in CAA36386. Ref.1

Secondary structure

.................................... 591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17812 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 0B04F9D9390C4152

FASTA59166,690
        10         20         30         40         50         60 
MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV 

        70         80         90        100        110        120 
LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK ERKGDYLGKT VQVVPHITDA 

       130        140        150        160        170        180 
IQEWVMRQAL IPVDEDGLEP QVCVIELGGT VGDIESMPFI EAFRQFQFKV KRENFCNIHV 

       190        200        210        220        230        240 
SLVPQPSSTG EQKTKPTQNS VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ 

       250        260        270        280        290        300 
VICVHDVSSI YRVPLLLEEQ GVVDYFLRRL DLPIERQPRK MLMKWKEMAD RYDRLLETCS 

       310        320        330        340        350        360 
IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDSA DLEPITSQEE PVRYHEAWQK 

       370        380        390        400        410        420 
LCSAHGVLVP GGFGVRGTEG KIQAIAWARN QKKPFLGVCL GMQLAVVEFS RNVLGWQDAN 

       430        440        450        460        470        480 
STEFDPTTSH PVVVDMPEHN PGQMGGTMRL GKRRTLFQTK NSVMRKLYGD ADYLEERHRH 

       490        500        510        520        530        540 
RFEVNPVWKK CLEEQGLKFV GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY 

       550        560        570        580        590 
FGLLLASVGR LSHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSINH D 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes."
Yamauchi M., Yamauchi N., Meuth M.
EMBO J. 9:2095-2099(1990) [PubMed: 2113467] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-571.
Tissue: Eye.
[5]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Expression of human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A."
Han G.-S., Sreenivas A., Choi M.-G., Chang Y.-F., Martin S.S., Baldwin E.P., Carman G.M.
J. Biol. Chem. 280:38328-38336(2005) [PubMed: 16179339] [Abstract]
Cited for: FUNCTION.
[7]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[8]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-573 AND SER-574, MASS SPECTROMETRY.
Tissue: Hepatoma.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573; SER-574 AND SER-575, MASS SPECTROMETRY.
Tissue: Platelet.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-573 AND SER-575, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573; SER-574; SER-575; THR-581 AND SER-587, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573; SER-574 AND SER-575, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, MASS SPECTROMETRY.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-574 AND SER-575, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, MASS SPECTROMETRY.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Crystal structure of the synthetase domain of human CTP synthetase."
Stenmark P., Kursula P., Arrowsmith C., Berglund H., Edwards A., Ehn M., Flodin S., Graslund S., Hammarstrom M., Hallberg B.M., Holmberg Schiavone L., Kotenyova T., Nilsson-ehle P., Ogg D., Persson C., Sagemark J., Schuler H., Sundstrom M. expand/collapse author list , Thorsell A.G., van den Berg S., Weigelt J., Nordlund P.
Submitted (NOV-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-272.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52142 mRNA. Translation: CAA36386.1.
AL391730 Genomic DNA. Translation: CAH72797.1.
CH471059 Genomic DNA. Translation: EAX07192.1.
CH471059 Genomic DNA. Translation: EAX07193.1.
BC009408 mRNA. Translation: AAH09408.1.
IPIIPI00290142.
PIRSYHUTP. S12791.
RefSeqNP_001896.2. NM_001905.2.
UniGeneHs.473087.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VO1X-ray2.80A/B1-273[»]
ProteinModelPortalP17812.
SMRP17812. Positions 1-273, 296-562.
ModBaseSearch...

Protein-protein interaction databases

IntActP17812. 7 interactions.
MINTMINT-3008801.
STRINGP17812.

PTM databases

PhosphoSiteP17812.

Polymorphism databases

DMDM20981706.

Proteomic databases

PeptideAtlasP17812.
PRIDEP17812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372616; ENSP00000361699; ENSG00000171793.
ENST00000372621; ENSP00000361704; ENSG00000171793.
GeneID1503.
KEGGhsa:1503.
UCSCuc001cgk.2. human.

Organism-specific databases

CTD1503.
GeneCardsGC01P041479.
H-InvDBHIX0000479.
HGNCHGNC:2519. CTPS.
HPACAB017111.
MIM123860. gene.
neXtProtNX_P17812.
PharmGKBPA27020.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08333.
GeneTreeENSGT00390000012473.
HOGENOMHBG597806.
HOVERGENHBG002243.
InParanoidP17812.
OMARVTMQKL.
OrthoDBEOG4868C4.
PhylomeDBP17812.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000171793-MONOMER.
BRENDA6.3.4.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP17812.
BgeeP17812.
CleanExHS_CTPS.
GenevestigatorP17812.
GermOnlineENSG00000171793. Homo sapiens.

Family and domain databases

InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE_1.
[Graphical view]
KOK01937.
PANTHERPTHR11550. PyrG_synth. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00130. L-Glutamine.
NextBio6221.
SOURCESearch...

Entry information

Entry namePYRG1_HUMAN
AccessionPrimary (citable) accession number: P17812
Secondary accession number(s): D3DPW1, Q5VW67, Q96GK6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 15, 2002
Last modified: January 25, 2012
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families