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P17812

- PYRG1_HUMAN

UniProt

P17812 - PYRG1_HUMAN

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Protein

CTP synthase 1

Gene

CTPS1

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

Functioni

This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity.2 Publications

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.2 Publications

Enzyme regulationi

Activated by GTP and inhibited by CTP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei399 – 3991For GATase activityBy similarity
Active sitei526 – 5261For GATase activityBy similarity
Active sitei528 – 5281For GATase activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
  2. B cell proliferation Source: UniProtKB
  3. CTP biosynthetic process Source: UniProtKB
  4. glutamine metabolic process Source: UniProtKB-KW
  5. nucleobase-containing compound metabolic process Source: ProtInc
  6. nucleobase-containing small molecule interconversion Source: Reactome
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. response to drug Source: ProtInc
  9. small molecule metabolic process Source: Reactome
  10. T cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Immunity, Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10382-MONOMER.
BRENDAi6.3.4.2. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00159; UER00277.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthase 1Curated (EC:6.3.4.22 Publications)
Alternative name(s):
CTP synthetase 1
UTP--ammonia ligase 1
Gene namesi
Name:CTPS1Imported
Synonyms:CTPSImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2519. CTPS1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 24 (IMD24) [MIM:615897]: A life-threatening immunodeficiency, characterized by an impaired capacity of activated T and B cells to proliferate in response to antigen receptor-mediated activation. Patients have early onset of severe chronic viral infections, mostly caused by herpes viruses, including EBV and varicella zooster virus (VZV), and also suffer from recurrent encapsulated bacterial infections, a spectrum of infections typical of a combined deficiency of adaptive immunity.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry. A unique and recessive G to C mutation probably affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a complete loss of the expression of the protein.1 Publication

Organism-specific databases

MIMi615897. phenotype.
PharmGKBiPA27020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591CTP synthase 1PRO_0000138275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei562 – 5621Phosphoserine1 Publication
Modified residuei568 – 5681Phosphoserine1 Publication
Modified residuei571 – 5711Phosphoserine2 Publications
Modified residuei573 – 5731Phosphoserine2 Publications
Modified residuei574 – 5741Phosphoserine3 Publications
Modified residuei575 – 5751Phosphoserine4 Publications
Modified residuei587 – 5871Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17812.
PaxDbiP17812.
PeptideAtlasiP17812.
PRIDEiP17812.

PTM databases

PhosphoSiteiP17812.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Up-regulated in T-cells and B-cells activated through the TCR and the BCR respectively (at protein level).1 Publication

Gene expression databases

BgeeiP17812.
CleanExiHS_CTPS.
ExpressionAtlasiP17812. baseline and differential.
GenevestigatoriP17812.

Organism-specific databases

HPAiCAB017111.
HPA051322.

Interactioni

Protein-protein interaction databases

BioGridi107883. 38 interactions.
IntActiP17812. 10 interactions.
MINTiMINT-3008801.
STRINGi9606.ENSP00000361699.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Beta strandi10 – 156
Helixi16 – 2914
Beta strandi34 – 407
Beta strandi87 – 893
Helixi90 – 10213
Turni103 – 1086
Helixi113 – 13018
Beta strandi134 – 1363
Beta strandi141 – 1477
Helixi154 – 1563
Helixi157 – 16913
Helixi172 – 1743
Beta strandi175 – 1828
Helixi195 – 20713
Beta strandi212 – 2176
Helixi224 – 23310
Helixi238 – 2403
Beta strandi241 – 2444
Helixi250 – 2523
Helixi253 – 2597
Helixi262 – 2709

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VO1X-ray2.80A/B1-273[»]
ProteinModelPortaliP17812.
SMRiP17812. Positions 1-273, 296-562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17812.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the CTP synthase family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0504.
GeneTreeiENSGT00390000012473.
HOGENOMiHOG000077514.
HOVERGENiHBG002243.
InParanoidiP17812.
KOiK01937.
OMAiDFLEERH.
OrthoDBiEOG7M3HZZ.
PhylomeDBiP17812.
TreeFamiTF300379.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P17812-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF
60 70 80 90 100
SPYEHGEVFV LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK
110 120 130 140 150
ERKGDYLGKT VQVVPHITDA IQEWVMRQAL IPVDEDGLEP QVCVIELGGT
160 170 180 190 200
VGDIESMPFI EAFRQFQFKV KRENFCNIHV SLVPQPSSTG EQKTKPTQNS
210 220 230 240 250
VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ VICVHDVSSI
260 270 280 290 300
YRVPLLLEEQ GVVDYFLRRL DLPIERQPRK MLMKWKEMAD RYDRLLETCS
310 320 330 340 350
IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDSA DLEPITSQEE
360 370 380 390 400
PVRYHEAWQK LCSAHGVLVP GGFGVRGTEG KIQAIAWARN QKKPFLGVCL
410 420 430 440 450
GMQLAVVEFS RNVLGWQDAN STEFDPTTSH PVVVDMPEHN PGQMGGTMRL
460 470 480 490 500
GKRRTLFQTK NSVMRKLYGD ADYLEERHRH RFEVNPVWKK CLEEQGLKFV
510 520 530 540 550
GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY FGLLLASVGR
560 570 580 590
LSHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSINH D
Length:591
Mass (Da):66,690
Last modified:May 15, 2002 - v2
Checksum:i0B04F9D9390C4152
GO
Isoform 2 (identifier: P17812-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-231: Missing.

Note: No experimental confirmation available.

Show »
Length:360
Mass (Da):41,220
Checksum:iA69483C20D884FBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051G → A in CAA36386. (PubMed:2113467)Curated
Sequence conflicti309 – 3091K → E in CAA36386. (PubMed:2113467)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti571 – 5711S → I.1 Publication
Corresponds to variant rs17856308 [ dbSNP | Ensembl ].
VAR_027055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 231231Missing in isoform 2. 1 PublicationVSP_055827Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52142 mRNA. Translation: CAA36386.1.
AK299122 mRNA. Translation: BAG61176.1.
AL391730 Genomic DNA. Translation: CAH72797.1.
CH471059 Genomic DNA. Translation: EAX07192.1.
CH471059 Genomic DNA. Translation: EAX07193.1.
BC009408 mRNA. Translation: AAH09408.1.
CCDSiCCDS459.1. [P17812-1]
PIRiS12791. SYHUTP.
RefSeqiNP_001896.2. NM_001905.3. [P17812-1]
XP_005270593.1. XM_005270536.1. [P17812-1]
XP_006710453.1. XM_006710390.1. [P17812-1]
XP_006710454.1. XM_006710391.1. [P17812-1]
UniGeneiHs.473087.

Genome annotation databases

EnsembliENST00000372616; ENSP00000361699; ENSG00000171793. [P17812-1]
ENST00000372621; ENSP00000361704; ENSG00000171793. [P17812-1]
GeneIDi1503.
KEGGihsa:1503.
UCSCiuc001cgk.4. human. [P17812-1]

Polymorphism databases

DMDMi20981706.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52142 mRNA. Translation: CAA36386.1 .
AK299122 mRNA. Translation: BAG61176.1 .
AL391730 Genomic DNA. Translation: CAH72797.1 .
CH471059 Genomic DNA. Translation: EAX07192.1 .
CH471059 Genomic DNA. Translation: EAX07193.1 .
BC009408 mRNA. Translation: AAH09408.1 .
CCDSi CCDS459.1. [P17812-1 ]
PIRi S12791. SYHUTP.
RefSeqi NP_001896.2. NM_001905.3. [P17812-1 ]
XP_005270593.1. XM_005270536.1. [P17812-1 ]
XP_006710453.1. XM_006710390.1. [P17812-1 ]
XP_006710454.1. XM_006710391.1. [P17812-1 ]
UniGenei Hs.473087.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VO1 X-ray 2.80 A/B 1-273 [» ]
ProteinModelPortali P17812.
SMRi P17812. Positions 1-273, 296-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107883. 38 interactions.
IntActi P17812. 10 interactions.
MINTi MINT-3008801.
STRINGi 9606.ENSP00000361699.

Chemistry

DrugBanki DB00130. L-Glutamine.

PTM databases

PhosphoSitei P17812.

Polymorphism databases

DMDMi 20981706.

Proteomic databases

MaxQBi P17812.
PaxDbi P17812.
PeptideAtlasi P17812.
PRIDEi P17812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372616 ; ENSP00000361699 ; ENSG00000171793 . [P17812-1 ]
ENST00000372621 ; ENSP00000361704 ; ENSG00000171793 . [P17812-1 ]
GeneIDi 1503.
KEGGi hsa:1503.
UCSCi uc001cgk.4. human. [P17812-1 ]

Organism-specific databases

CTDi 1503.
GeneCardsi GC01P041445.
H-InvDB HIX0000479.
HGNCi HGNC:2519. CTPS1.
HPAi CAB017111.
HPA051322.
MIMi 123860. gene.
615897. phenotype.
neXtProti NX_P17812.
PharmGKBi PA27020.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0504.
GeneTreei ENSGT00390000012473.
HOGENOMi HOG000077514.
HOVERGENi HBG002243.
InParanoidi P17812.
KOi K01937.
OMAi DFLEERH.
OrthoDBi EOG7M3HZZ.
PhylomeDBi P17812.
TreeFami TF300379.

Enzyme and pathway databases

UniPathwayi UPA00159 ; UER00277 .
BioCyci MetaCyc:HS10382-MONOMER.
BRENDAi 6.3.4.2. 2681.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTracei P17812.
GeneWikii CTP_synthase_1.
GenomeRNAii 1503.
NextBioi 35474308.
PROi P17812.
SOURCEi Search...

Gene expression databases

Bgeei P17812.
CleanExi HS_CTPS.
ExpressionAtlasi P17812. baseline and differential.
Genevestigatori P17812.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPi MF_01227. PyrG.
InterProi IPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11550. PTHR11550. 1 hit.
Pfami PF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00337. PyrG. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  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] (ISOFORM 2).
  3. "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.
    , 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] [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] (ISOFORM 1), VARIANT ILE-571.
    Tissue: Eye.
  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, CATALYTIC ACTIVITY, PATHWAY.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  10. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573; SER-574; SER-575 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-574 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-574 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-562; SER-573 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, INDUCTION, INVOLVEMENT IN IMD24.
  21. "Structure of the synthetase domain of human CTP synthetase, a target for anticancer therapy."
    Kursula P., Flodin S., Ehn M., Hammarstrom M., Schuler H., Nordlund P., Stenmark P.
    Acta Crystallogr. F 62:613-617(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-272.

Entry informationi

Entry nameiPYRG1_HUMAN
AccessioniPrimary (citable) accession number: P17812
Secondary accession number(s): B4DR64
, D3DPW1, Q5VW67, Q96GK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 15, 2002
Last modified: October 29, 2014
This is version 157 of the entry and version 2 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3