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P17812

- PYRG1_HUMAN

UniProt

P17812 - PYRG1_HUMAN

Protein

CTP synthase 1

Gene

CTPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.1 Publication

    Catalytic activityi

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

    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. CTP biosynthetic process Source: UniProtKB
    3. glutamine metabolic process Source: UniProtKB-KW
    4. nucleobase-containing compound metabolic process Source: ProtInc
    5. nucleobase-containing small molecule interconversion Source: Reactome
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. response to drug Source: ProtInc
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    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 1 (EC:6.3.4.2)
    Alternative name(s):
    CTP synthetase 1
    UTP--ammonia ligase 1
    Gene namesi
    Name:CTPS1
    Synonyms:CTPS
    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

    Pathology & Biotechi

    Organism-specific databases

    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

    Gene expression databases

    ArrayExpressiP17812.
    BgeeiP17812.
    CleanExiHS_CTPS.
    GenevestigatoriP17812.

    Organism-specific databases

    HPAiCAB017111.
    HPA051322.

    Interactioni

    Protein-protein interaction databases

    BioGridi107883. 35 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.
    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

    MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF    50
    SPYEHGEVFV LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK 100
    ERKGDYLGKT VQVVPHITDA IQEWVMRQAL IPVDEDGLEP QVCVIELGGT 150
    VGDIESMPFI EAFRQFQFKV KRENFCNIHV SLVPQPSSTG EQKTKPTQNS 200
    VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ VICVHDVSSI 250
    YRVPLLLEEQ GVVDYFLRRL DLPIERQPRK MLMKWKEMAD RYDRLLETCS 300
    IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDSA DLEPITSQEE 350
    PVRYHEAWQK LCSAHGVLVP GGFGVRGTEG KIQAIAWARN QKKPFLGVCL 400
    GMQLAVVEFS RNVLGWQDAN STEFDPTTSH PVVVDMPEHN PGQMGGTMRL 450
    GKRRTLFQTK NSVMRKLYGD ADYLEERHRH RFEVNPVWKK CLEEQGLKFV 500
    GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY FGLLLASVGR 550
    LSHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSINH D 591
    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.
    PIRiS12791. SYHUTP.
    RefSeqiNP_001896.2. NM_001905.2.
    XP_005270593.1. XM_005270536.1.
    XP_006710453.1. XM_006710390.1.
    XP_006710454.1. XM_006710391.1.
    UniGeneiHs.473087.

    Genome annotation databases

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

    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.
    PIRi S12791. SYHUTP.
    RefSeqi NP_001896.2. NM_001905.2.
    XP_005270593.1. XM_005270536.1.
    XP_006710453.1. XM_006710390.1.
    XP_006710454.1. XM_006710391.1.
    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. 35 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.

    Organism-specific databases

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

    Phylogenomic databases

    eggNOGi COG0504.
    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 6221.
    PROi P17812.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17812.
    Bgeei P17812.
    CleanExi HS_CTPS.
    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

    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.
    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: 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 1, 2014
    This is version 156 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