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Q9NRF8 (PYRG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTP synthase 2

EC=6.3.4.2
Alternative name(s):
CTP synthetase 2
UTP--ammonia ligase 2
Gene names
Name:CTPS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 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. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. Ref.1 Ref.6

Catalytic activity

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586CTP synthase 2
PRO_0000247033

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 residue5681Phosphoserine Ref.8 Ref.9 Ref.11
Modified residue5711Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11
Modified residue5741Phosphoserine Ref.8 Ref.9

Experimental info

Sequence conflict2201T → S in BAB14814. Ref.2
Sequence conflict2331F → L in BAB14607. Ref.2
Sequence conflict3041V → A in BAB14607. Ref.2

Secondary structure

..................................................................................... 586
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NRF8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AC1CF2E67D89741B

FASTA58665,678
        10         20         30         40         50         60 
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV 

        70         80         90        100        110        120 
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA 

       130        140        150        160        170        180 
VQEWVMNQAK VPVDGNKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV 

       190        200        210        220        230        240 
SLVPQLSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ 

       250        260        270        280        290        300 
VICIHDVSST YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS 

       310        320        330        340        350        360 
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED PVKFHEAWQK 

       370        380        390        400        410        420 
LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL GMQLAVIEFA RNCLNLKDAD 

       430        440        450        460        470        480 
STEFRPNAPV PLVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH 

       490        500        510        520        530        540 
RFEVNPNLIK QFEQNDLSFV GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY 

       550        560        570        580 
LGLLLAATGN LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a cDNA encoding an isoform of human CTP synthetase."
van Kuilenburg A.B.P., Meinsma R., Vreken P., Waterham H.R., van Gennip A.H.
Biochim. Biophys. Acta 1492:548-552(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Retinoblastoma.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Testis.
[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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF226667 mRNA. Translation: AAF91241.1.
AK023549 mRNA. Translation: BAB14607.1.
AK024070 mRNA. Translation: BAB14814.1.
AK125332 mRNA. Translation: BAG54184.1.
AK125348 mRNA. Translation: BAG54188.1.
AL445467, AC073909 Genomic DNA. Translation: CAI40086.1.
CH471074 Genomic DNA. Translation: EAW98912.1.
BC006256 mRNA. Translation: AAH06256.2.
BC034986 mRNA. Translation: AAH34986.1.
RefSeqNP_001137474.1. NM_001144002.1.
NP_062831.3. NM_019857.4.
NP_787055.1. NM_175859.2.
XP_005274619.1. XM_005274562.1.
XP_005274620.1. XM_005274563.1.
UniGeneHs.227049.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4UX-ray2.30A297-562[»]
2VKTX-ray2.50A297-562[»]
3IHLX-ray2.80A/B1-275[»]
ProteinModelPortalQ9NRF8.
SMRQ9NRF8. Positions 1-273, 297-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121144. 22 interactions.
IntActQ9NRF8. 6 interactions.
MINTMINT-1443035.
STRING9606.ENSP00000352222.

PTM databases

PhosphoSiteQ9NRF8.

Polymorphism databases

DMDM74752919.

Proteomic databases

PaxDbQ9NRF8.
PRIDEQ9NRF8.

Protocols and materials databases

DNASU56474.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359276; ENSP00000352222; ENSG00000047230.
ENST00000380241; ENSP00000369590; ENSG00000047230.
ENST00000443824; ENSP00000401264; ENSG00000047230.
GeneID56474.
KEGGhsa:56474.
UCSCuc004cxk.3. human.

Organism-specific databases

CTD56474.
GeneCardsGC0XM016606.
HGNCHGNC:2520. CTPS2.
HPAHPA017437.
MIM300380. gene.
neXtProtNX_Q9NRF8.
PharmGKBPA27021.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0504.
HOGENOMHOG000077514.
HOVERGENHBG002243.
InParanoidQ9NRF8.
KOK01937.
OMAFEVNPNL.
OrthoDBEOG7M3HZZ.
TreeFamTF300379.

Enzyme and pathway databases

BioCycMetaCyc:HS00585-MONOMER.
BRENDA6.3.4.2. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00159; UER00277.

Gene expression databases

BgeeQ9NRF8.
CleanExHS_CTPS2.
GenevestigatorQ9NRF8.

Family and domain databases

InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11550. PTHR11550. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NRF8.
GeneWikiCTPS2.
GenomeRNAi56474.
NextBio62001.
PROQ9NRF8.
SOURCESearch...

Entry information

Entry namePYRG2_HUMAN
AccessionPrimary (citable) accession number: Q9NRF8
Secondary accession number(s): B3KWM2 expand/collapse secondary AC list , Q9BRI0, Q9H809, Q9H8K9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 111 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome X

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