Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NRF8

- PYRG2_HUMAN

UniProt

Q9NRF8 - PYRG2_HUMAN

Protein

CTP synthase 2

Gene

CTPS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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.

    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

    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.
    GenevestigatoriQ9NRF8.

    Organism-specific databases

    HPAiHPA017437.

    Interactioni

    Protein-protein interaction databases

    BioGridi121144. 23 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 – 87
    Beta strandi10 – 156
    Helixi16 – 2813
    Turni29 – 313
    Beta strandi34 – 407
    Beta strandi87 – 893
    Helixi90 – 10213
    Turni103 – 1086
    Helixi113 – 12917
    Beta strandi141 – 1477
    Helixi154 – 1563
    Helixi157 – 16913
    Helixi172 – 1743
    Beta strandi175 – 1828
    Turni187 – 1893
    Helixi195 – 20612
    Beta strandi212 – 2209
    Helixi224 – 23310
    Helixi238 – 2403
    Beta strandi241 – 2455
    Helixi252 – 2598
    Helixi262 – 2709
    Beta strandi297 – 30610
    Helixi312 – 3143
    Helixi315 – 32713
    Beta strandi330 – 3389
    Helixi339 – 3424
    Helixi344 – 3496
    Helixi351 – 36313
    Beta strandi365 – 3695
    Helixi378 – 39013
    Beta strandi395 – 3984
    Helixi400 – 41314
    Beta strandi419 – 4224
    Beta strandi429 – 4357
    Beta strandi449 – 45810
    Helixi463 – 4675
    Beta strandi472 – 4809
    Beta strandi482 – 4843
    Helixi486 – 4883
    Helixi490 – 4923
    Beta strandi495 – 5039
    Beta strandi508 – 51811
    Beta strandi520 – 5267
    Helixi527 – 5304
    Helixi538 – 54811
    Helixi551 – 5566

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000077514.
    HOVERGENiHBG002243.
    InParanoidiQ9NRF8.
    KOiK01937.
    OMAiCDIDKNA.
    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

    MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF    50
    SPYEHGEVFV LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK 100
    ERRGDYLGKT VQVVPHITDA VQEWVMNQAK VPVDGNKEEP QICVIELGGT 150
    IGDIEGMPFV EAFRQFQFKA KRENFCNIHV SLVPQLSATG EQKTKPTQNS 200
    VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ VICIHDVSST 250
    YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS 300
    IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED 350
    PVKFHEAWQK LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL 400
    GMQLAVIEFA RNCLNLKDAD STEFRPNAPV PLVIDMPEHN PGNLGGTMRL 450
    GIRRTVFKTE NSILRKLYGD VPFIEERHRH RFEVNPNLIK QFEQNDLSFV 500
    GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY LGLLLAATGN 550
    LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS 586
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14175.1.
    RefSeqi NP_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.
    UniGenei Hs.227049.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V4U X-ray 2.30 A 297-562 [» ]
    2VKT X-ray 2.50 A 297-562 [» ]
    3IHL X-ray 2.80 A/B 1-275 [» ]
    ProteinModelPortali Q9NRF8.
    SMRi Q9NRF8. Positions 1-273, 297-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121144. 23 interactions.
    IntActi Q9NRF8. 6 interactions.
    MINTi MINT-1443035.
    STRINGi 9606.ENSP00000352222.

    PTM databases

    PhosphoSitei Q9NRF8.

    Polymorphism databases

    DMDMi 74752919.

    Proteomic databases

    MaxQBi Q9NRF8.
    PaxDbi Q9NRF8.
    PRIDEi Q9NRF8.

    Protocols and materials databases

    DNASUi 56474.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359276 ; ENSP00000352222 ; ENSG00000047230 .
    ENST00000380241 ; ENSP00000369590 ; ENSG00000047230 .
    ENST00000443824 ; ENSP00000401264 ; ENSG00000047230 .
    GeneIDi 56474.
    KEGGi hsa:56474.
    UCSCi uc004cxk.3. human.

    Organism-specific databases

    CTDi 56474.
    GeneCardsi GC0XM016606.
    HGNCi HGNC:2520. CTPS2.
    HPAi HPA017437.
    MIMi 300380. gene.
    neXtProti NX_Q9NRF8.
    PharmGKBi PA27021.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0504.
    HOGENOMi HOG000077514.
    HOVERGENi HBG002243.
    InParanoidi Q9NRF8.
    KOi K01937.
    OMAi CDIDKNA.
    OrthoDBi EOG7M3HZZ.
    PhylomeDBi Q9NRF8.
    TreeFami TF300379.

    Enzyme and pathway databases

    UniPathwayi UPA00159 ; UER00277 .
    BioCyci MetaCyc:HS00585-MONOMER.
    BRENDAi 6.3.4.2. 2681.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    EvolutionaryTracei Q9NRF8.
    GeneWikii CTPS2.
    GenomeRNAii 56474.
    NextBioi 62001.
    PROi Q9NRF8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRF8.
    CleanExi HS_CTPS2.
    Genevestigatori Q9NRF8.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    3.40.50.880. 1 hit.
    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. 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: October 1, 2014
    This is version 117 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