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Protein

CTP synthase 2

Gene

CTPS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei399 – 3991For GATase activityPROSITE-ProRule annotation
Active sitei526 – 5261For GATase activityPROSITE-ProRule annotation
Active sitei528 – 5281For GATase activityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. CTP synthase activity Source: Reactome

GO - Biological processi

  1. 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
  2. glutamine metabolic process Source: UniProtKB-KW
  3. nucleobase-containing small molecule interconversion Source: Reactome
  4. nucleobase-containing small molecule metabolic process Source: Reactome
  5. pyrimidine nucleotide metabolic process Source: ProtInc
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00585-MONOMER.
BRENDAi6.3.4.2. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00159; UER00277.

Protein family/group databases

MEROPSiC26.964.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthase 2 (EC:6.3.4.2)
Alternative name(s):
CTP synthetase 2
UTP--ammonia ligase 2
Gene namesi
Name:CTPS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2520. CTPS2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586CTP synthase 2PRO_0000247033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei568 – 5681Phosphoserine3 Publications
Modified residuei571 – 5711Phosphoserine4 Publications
Modified residuei574 – 5741Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRF8.
PaxDbiQ9NRF8.
PRIDEiQ9NRF8.

PTM databases

PhosphoSiteiQ9NRF8.

Expressioni

Gene expression databases

BgeeiQ9NRF8.
CleanExiHS_CTPS2.
ExpressionAtlasiQ9NRF8. baseline and differential.
GenevestigatoriQ9NRF8.

Organism-specific databases

HPAiHPA017437.

Interactioni

Protein-protein interaction databases

BioGridi121144. 26 interactions.
IntActiQ9NRF8. 6 interactions.
MINTiMINT-1443035.
STRINGi9606.ENSP00000352222.

Structurei

Secondary structure

1
586
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi10 – 156Combined sources
Helixi16 – 2813Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 407Combined sources
Beta strandi87 – 893Combined sources
Helixi90 – 10213Combined sources
Turni103 – 1086Combined sources
Helixi113 – 12917Combined sources
Beta strandi141 – 1477Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 16913Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 1828Combined sources
Turni187 – 1893Combined sources
Helixi195 – 20612Combined sources
Beta strandi212 – 2209Combined sources
Helixi224 – 23310Combined sources
Helixi238 – 2403Combined sources
Beta strandi241 – 2455Combined sources
Helixi252 – 2598Combined sources
Helixi262 – 2709Combined sources
Beta strandi297 – 3059Combined sources
Helixi312 – 3143Combined sources
Helixi315 – 32713Combined sources
Beta strandi330 – 3389Combined sources
Helixi339 – 3424Combined sources
Helixi344 – 3496Combined sources
Helixi351 – 36212Combined sources
Beta strandi365 – 3695Combined sources
Helixi378 – 39013Combined sources
Beta strandi395 – 3984Combined sources
Helixi400 – 41314Combined sources
Beta strandi419 – 4213Combined sources
Turni422 – 4243Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi449 – 45810Combined sources
Helixi463 – 4675Combined sources
Beta strandi472 – 4809Combined sources
Beta strandi482 – 4843Combined sources
Helixi486 – 4927Combined sources
Beta strandi495 – 5028Combined sources
Beta strandi509 – 5146Combined sources
Beta strandi520 – 5267Combined sources
Helixi527 – 5304Combined sources
Helixi538 – 54710Combined sources
Turni551 – 5533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4UX-ray2.30A297-562[»]
2VKTX-ray2.50A297-562[»]
3IHLX-ray2.80A/B1-275[»]
ProteinModelPortaliQ9NRF8.
SMRiQ9NRF8. Positions 1-273, 297-562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRF8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini300 – 554255Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CTP synthase family.Curated
Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0504.
GeneTreeiENSGT00390000012473.
HOGENOMiHOG000077514.
HOVERGENiHBG002243.
InParanoidiQ9NRF8.
KOiK01937.
OMAiFEVNPNL.
OrthoDBiEOG7M3HZZ.
PhylomeDBiQ9NRF8.
TreeFamiTF300379.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRF8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF
60 70 80 90 100
SPYEHGEVFV LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK
110 120 130 140 150
ERRGDYLGKT VQVVPHITDA VQEWVMNQAK VPVDGNKEEP QICVIELGGT
160 170 180 190 200
IGDIEGMPFV EAFRQFQFKA KRENFCNIHV SLVPQLSATG EQKTKPTQNS
210 220 230 240 250
VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ VICIHDVSST
260 270 280 290 300
YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS
310 320 330 340 350
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED
360 370 380 390 400
PVKFHEAWQK LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL
410 420 430 440 450
GMQLAVIEFA RNCLNLKDAD STEFRPNAPV PLVIDMPEHN PGNLGGTMRL
460 470 480 490 500
GIRRTVFKTE NSILRKLYGD VPFIEERHRH RFEVNPNLIK QFEQNDLSFV
510 520 530 540 550
GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY LGLLLAATGN
560 570 580
LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS
Length:586
Mass (Da):65,678
Last modified:October 1, 2000 - v1
Checksum:iAC1CF2E67D89741B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201T → S in BAB14814. (PubMed:14702039)Curated
Sequence conflicti233 – 2331F → L in BAB14607. (PubMed:14702039)Curated
Sequence conflicti304 – 3041V → A in BAB14607. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14175.1.
RefSeqiNP_001137474.1. NM_001144002.1.
NP_062831.3. NM_019857.4.
NP_787055.1. NM_175859.2.
XP_005274619.1. XM_005274562.1.
XP_006724566.1. XM_006724503.1.
UniGeneiHs.227049.

Genome annotation databases

EnsembliENST00000359276; ENSP00000352222; ENSG00000047230.
ENST00000380241; ENSP00000369590; ENSG00000047230.
ENST00000443824; ENSP00000401264; ENSG00000047230.
GeneIDi56474.
KEGGihsa:56474.
UCSCiuc004cxk.3. human.

Polymorphism databases

DMDMi74752919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14175.1.
RefSeqiNP_001137474.1. NM_001144002.1.
NP_062831.3. NM_019857.4.
NP_787055.1. NM_175859.2.
XP_005274619.1. XM_005274562.1.
XP_006724566.1. XM_006724503.1.
UniGeneiHs.227049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4UX-ray2.30A297-562[»]
2VKTX-ray2.50A297-562[»]
3IHLX-ray2.80A/B1-275[»]
ProteinModelPortaliQ9NRF8.
SMRiQ9NRF8. Positions 1-273, 297-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121144. 26 interactions.
IntActiQ9NRF8. 6 interactions.
MINTiMINT-1443035.
STRINGi9606.ENSP00000352222.

Protein family/group databases

MEROPSiC26.964.

PTM databases

PhosphoSiteiQ9NRF8.

Polymorphism databases

DMDMi74752919.

Proteomic databases

MaxQBiQ9NRF8.
PaxDbiQ9NRF8.
PRIDEiQ9NRF8.

Protocols and materials databases

DNASUi56474.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359276; ENSP00000352222; ENSG00000047230.
ENST00000380241; ENSP00000369590; ENSG00000047230.
ENST00000443824; ENSP00000401264; ENSG00000047230.
GeneIDi56474.
KEGGihsa:56474.
UCSCiuc004cxk.3. human.

Organism-specific databases

CTDi56474.
GeneCardsiGC0XM016606.
HGNCiHGNC:2520. CTPS2.
HPAiHPA017437.
MIMi300380. gene.
neXtProtiNX_Q9NRF8.
PharmGKBiPA27021.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0504.
GeneTreeiENSGT00390000012473.
HOGENOMiHOG000077514.
HOVERGENiHBG002243.
InParanoidiQ9NRF8.
KOiK01937.
OMAiFEVNPNL.
OrthoDBiEOG7M3HZZ.
PhylomeDBiQ9NRF8.
TreeFamiTF300379.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.
BioCyciMetaCyc:HS00585-MONOMER.
BRENDAi6.3.4.2. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSiCTPS2. human.
EvolutionaryTraceiQ9NRF8.
GeneWikiiCTPS2.
GenomeRNAii56474.
NextBioi62001.
PROiQ9NRF8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRF8.
CleanExiHS_CTPS2.
ExpressionAtlasiQ9NRF8. baseline and differential.
GenevestigatoriQ9NRF8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiPYRG2_HUMAN
AccessioniPrimary (citable) accession number: Q9NRF8
Secondary accession number(s): B3KWM2
, Q9BRI0, Q9H809, Q9H8K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.