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Protein

Thymidylate synthase

Gene

Ts

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

  • dTMP biosynthetic process Source: InterPro
  • dTTP biosynthetic process Source: UniProtKB-UniPathway
  • neurogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

ReactomeiREACT_282432. G1/S-Specific Transcription.
REACT_310550. Pyrimidine biosynthesis.
REACT_345084. 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 Componenti: 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.
ExpressionAtlasiO76511. differential.
GenevisibleiO76511. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi59719. 1 interaction.
DIPiDIP-20012N.
IntActiO76511. 1 interaction.
MINTiMINT-326941.
STRINGi7227.FBpp0077363.

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.
OMAiNEWADEN.
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

        10         20         30         40         50
MVLTPTKDGP DQESMPLPAD NGESPSKQQA PVNRDEMHYL DLLRHIIANG
60 70 80 90 100
EQRMDRTEVG TLSVFGSQMR FDMRNSFPLL TTKRVFFRAV AEELLWFVAG
110 120 130 140 150
KTDAKLLQAK NVHIWDGNSS REFLDKMGFT GRAVGDLGPV YGFQWRHFGA
160 170 180 190 200
QYGTCDDDYS GKGIDQLRQV IDTIRNNPSD RRIIMSAWNP LDIPKMALPP
210 220 230 240 250
CHCLAQFYVS EKRGELSCQL YQRSADMGLG VPFNIASYAL LTHMIAHVTG
260 270 280 290 300
LKPGDFVHTM GDTHVYLNHV EPLKEQLERT PRPFPKLIIK RQVQDIEDFR
310 320
FEDFQIVDYN PHPKIQMDMA V
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 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF073994 Genomic DNA. Translation: AAC27622.1.
AE014134 Genomic DNA. Translation: AAF51176.1.
RefSeqiNP_001285570.1. NM_001298641.1.
NP_477367.1. NM_058019.4.
UniGeneiDm.30804.

Genome annotation databases

EnsemblMetazoaiFBtr0077679; FBpp0077363; FBgn0024920.
FBtr0343784; FBpp0310349; FBgn0024920.
GeneIDi33499.
KEGGidme:Dmel_CG3181.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF073994 Genomic DNA. Translation: AAC27622.1.
AE014134 Genomic DNA. Translation: AAF51176.1.
RefSeqiNP_001285570.1. NM_001298641.1.
NP_477367.1. NM_058019.4.
UniGeneiDm.30804.

3D structure databases

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

Protein-protein interaction databases

BioGridi59719. 1 interaction.
DIPiDIP-20012N.
IntActiO76511. 1 interaction.
MINTiMINT-326941.
STRINGi7227.FBpp0077363.

Proteomic databases

PaxDbiO76511.
PRIDEiO76511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077679; FBpp0077363; FBgn0024920.
FBtr0343784; FBpp0310349; FBgn0024920.
GeneIDi33499.
KEGGidme:Dmel_CG3181.

Organism-specific databases

CTDi33499.
FlyBaseiFBgn0024920. Ts.

Phylogenomic databases

eggNOGiCOG0207.
InParanoidiO76511.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG725DHX.
PhylomeDBiO76511.

Enzyme and pathway databases

UniPathwayiUPA00575.
ReactomeiREACT_282432. G1/S-Specific Transcription.
REACT_310550. Pyrimidine biosynthesis.
REACT_345084. E2F mediated regulation of DNA replication.

Miscellaneous databases

GenomeRNAii33499.
NextBioi783907.
PROiO76511.

Gene expression databases

BgeeiO76511.
ExpressionAtlasiO76511. differential.
GenevisibleiO76511. DM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 111 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

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.