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O76511

- TYSY_DROME

UniProt

O76511 - TYSY_DROME

Protein

Thymidylate synthase

Gene

Ts

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (04 May 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei201 – 2011By similarity

    GO - Molecular functioni

    1. thymidylate synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. dTMP biosynthetic process Source: InterPro
    2. dTTP biosynthetic process Source: UniProtKB-UniPathway
    3. neurogenesis Source: FlyBase

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_180285. G1/S-Specific Transcription.
    REACT_204719. Pyrimidine biosynthesis.
    REACT_209388. E2F mediated regulation of DNA replication.
    UniPathwayiUPA00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidylate synthase (EC:2.1.1.45)
    Short name:
    TS
    Short name:
    TSase
    Gene namesi
    Name:Ts
    ORF Names:CG3181
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0024920. Ts.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321Thymidylate synthasePRO_0000140905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei26 – 261Phosphoserine1 Publication
    Modified residuei39 – 391Phosphotyrosine1 Publication
    Modified residuei208 – 2081Phosphotyrosine1 Publication
    Modified residuei210 – 2101Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO76511.
    PRIDEiO76511.

    Expressioni

    Gene expression databases

    BgeeiO76511.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi59719. 1 interaction.
    DIPiDIP-20012N.
    MINTiMINT-326941.

    Structurei

    3D structure databases

    ProteinModelPortaliO76511.
    SMRiO76511. Positions 36-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymidylate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0207.
    InParanoidiO76511.
    KOiK00560.
    OMAiAQWRHWE.
    OrthoDBiEOG725DHX.
    PhylomeDBiO76511.

    Family and domain databases

    Gene3Di3.30.572.10. 1 hit.
    HAMAPiMF_00008. Thymidy_synth_bact.
    InterProiIPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view]
    PfamiPF00303. Thymidylat_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00108. THYMDSNTHASE.
    SUPFAMiSSF55831. SSF55831. 1 hit.
    TIGRFAMsiTIGR03284. thym_sym. 1 hit.
    PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O76511-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLTPTKDGP DQESMPLPAD NGESPSKQQA PVNRDEMHYL DLLRHIIANG    50
    EQRMDRTEVG TLSVFGSQMR FDMRNSFPLL TTKRVFFRAV AEELLWFVAG 100
    KTDAKLLQAK NVHIWDGNSS REFLDKMGFT GRAVGDLGPV YGFQWRHFGA 150
    QYGTCDDDYS GKGIDQLRQV IDTIRNNPSD RRIIMSAWNP LDIPKMALPP 200
    CHCLAQFYVS EKRGELSCQL YQRSADMGLG VPFNIASYAL LTHMIAHVTG 250
    LKPGDFVHTM GDTHVYLNHV EPLKEQLERT PRPFPKLIIK RQVQDIEDFR 300
    FEDFQIVDYN PHPKIQMDMA V 321
    Length:321
    Mass (Da):36,657
    Last modified:May 4, 2001 - v2
    Checksum:iDCBC920153990CFE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti193 – 1931I → M in AAC27622. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073994 Genomic DNA. Translation: AAC27622.1.
    AE014134 Genomic DNA. Translation: AAF51176.1.
    RefSeqiNP_477367.1. NM_058019.3.
    UniGeneiDm.30804.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077679; FBpp0077363; FBgn0024920.
    GeneIDi33499.
    KEGGidme:Dmel_CG3181.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073994 Genomic DNA. Translation: AAC27622.1 .
    AE014134 Genomic DNA. Translation: AAF51176.1 .
    RefSeqi NP_477367.1. NM_058019.3.
    UniGenei Dm.30804.

    3D structure databases

    ProteinModelPortali O76511.
    SMRi O76511. Positions 36-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59719. 1 interaction.
    DIPi DIP-20012N.
    MINTi MINT-326941.

    Proteomic databases

    PaxDbi O76511.
    PRIDEi O76511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077679 ; FBpp0077363 ; FBgn0024920 .
    GeneIDi 33499.
    KEGGi dme:Dmel_CG3181.

    Organism-specific databases

    CTDi 33499.
    FlyBasei FBgn0024920. Ts.

    Phylogenomic databases

    eggNOGi COG0207.
    InParanoidi O76511.
    KOi K00560.
    OMAi AQWRHWE.
    OrthoDBi EOG725DHX.
    PhylomeDBi O76511.

    Enzyme and pathway databases

    UniPathwayi UPA00575 .
    Reactomei REACT_180285. G1/S-Specific Transcription.
    REACT_204719. Pyrimidine biosynthesis.
    REACT_209388. E2F mediated regulation of DNA replication.

    Miscellaneous databases

    GenomeRNAii 33499.
    NextBioi 783907.
    PROi O76511.

    Gene expression databases

    Bgeei O76511.

    Family and domain databases

    Gene3Di 3.30.572.10. 1 hit.
    HAMAPi MF_00008. Thymidy_synth_bact.
    InterProi IPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view ]
    Pfami PF00303. Thymidylat_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00108. THYMDSNTHASE.
    SUPFAMi SSF55831. SSF55831. 1 hit.
    TIGRFAMsi TIGR03284. thym_sym. 1 hit.
    PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization of the Drosophlia 23C genetic interval: identification of 3 genes in the 10Kb region surrounding the RRP1 gene."
      Tsoi S.C.M., Huang S.M., Sander M.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-208 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-26 AND TYR-39, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiTYSY_DROME
    AccessioniPrimary (citable) accession number: O76511
    Secondary accession number(s): Q9VQJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 4, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3