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Protein

Thymidylate synthase

Gene

Tyms

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891By similarity

GO - Molecular functioni

  1. cofactor binding Source: Ensembl
  2. drug binding Source: Ensembl
  3. folic acid binding Source: Ensembl
  4. mRNA binding Source: Ensembl
  5. nucleotide binding Source: Ensembl
  6. thymidylate synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. aging Source: Ensembl
  2. cartilage development Source: Ensembl
  3. circadian rhythm Source: Ensembl
  4. developmental growth Source: Ensembl
  5. dTMP biosynthetic process Source: InterPro
  6. dTTP biosynthetic process Source: UniProtKB-UniPathway
  7. dUMP metabolic process Source: Ensembl
  8. immortalization of host cell by virus Source: Ensembl
  9. intestinal epithelial cell maturation Source: Ensembl
  10. organ regeneration Source: Ensembl
  11. response to cytokine Source: Ensembl
  12. response to drug Source: Ensembl
  13. response to ethanol Source: Ensembl
  14. response to folic acid Source: Ensembl
  15. response to glucocorticoid Source: Ensembl
  16. response to organophosphorus Source: Ensembl
  17. response to progesterone Source: Ensembl
  18. response to toxic substance Source: Ensembl
  19. response to vitamin A Source: Ensembl
  20. tetrahydrofolate metabolic process Source: Ensembl
  21. uracil metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

ReactomeiREACT_198608. G1/S-Specific Transcription.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_238763. Pyrimidine biosynthesis.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase (EC:2.1.1.45)
Short name:
TS
Short name:
TSase
Gene namesi
Name:Tyms
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:98878. Tyms.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion matrix By similarity. Mitochondrion inner membrane By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrion Source: UniProtKB
  5. nucleolus Source: Ensembl
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 307306Thymidylate synthasePRO_0000140902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07607.
PaxDbiP07607.
PRIDEiP07607.

2D gel databases

REPRODUCTION-2DPAGEP07607.

PTM databases

PhosphoSiteiP07607.

Expressioni

Gene expression databases

BgeeiP07607.
CleanExiMM_TYMS.
ExpressionAtlasiP07607. baseline and differential.
GenevestigatoriP07607.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
307
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3714Combined sources
Beta strandi39 – 413Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 6012Combined sources
Beta strandi62 – 643Combined sources
Beta strandi69 – 713Combined sources
Helixi75 – 8612Combined sources
Helixi92 – 965Combined sources
Turni97 – 993Combined sources
Turni102 – 1076Combined sources
Helixi109 – 1146Combined sources
Helixi129 – 1357Combined sources
Helixi154 – 16411Combined sources
Beta strandi172 – 1743Combined sources
Turni178 – 1803Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi189 – 19810Combined sources
Beta strandi201 – 21212Combined sources
Turni213 – 2153Combined sources
Helixi216 – 23520Combined sources
Beta strandi238 – 25215Combined sources
Helixi253 – 2553Combined sources
Helixi256 – 2638Combined sources
Beta strandi272 – 2754Combined sources
Helixi282 – 2843Combined sources
Helixi287 – 2893Combined sources
Beta strandi290 – 2945Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IHIX-ray1.94A/B1-307[»]
4E5OX-ray1.70A/B/C/D/E/F1-307[»]
4EB4X-ray1.74A/B/C/D1-307[»]
4EINX-ray1.75A/B1-307[»]
4EZ8X-ray1.17A1-307[»]
ProteinModelPortaliP07607.
SMRiP07607. Positions 21-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07607.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP07607.
KOiK00560.
OMAiNEWADEN.
PhylomeDBiP07607.
TreeFamiTF353027.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVVGSELQS DAQQLSAEAP RHGELQYLRQ VEHILRCGFK KEDRTGTGTL
60 70 80 90 100
SVFGMQARYS LRDEFPLLTT KRVFWKGVLE ELLWFIKGST NAKELSSKGV
110 120 130 140 150
RIWDANGSRD FLDSLGFSAR QEGDLGPVYG FQWRHFGAEY KDMDSDYSGQ
160 170 180 190 200
GVDQLQKVID TIKTNPDDRR IIMCAWNPKD LPLMALPPCH ALCQFYVVNG
210 220 230 240 250
ELSCQLYQRS GDMGLGVPFN IASYALLTYM IAHITGLQPG DFVHTLGDAH
260 270 280 290 300
IYLNHIEPLK IQLQREPRPF PKLKILRKVE TIDDFKVEDF QIEGYNPHPT

IKMEMAV
Length:307
Mass (Da):34,958
Last modified:April 1, 1988 - v1
Checksum:iE4930618C487FD5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13019 mRNA. Translation: AAA40439.1.
M13352
, J02617, M13347, M13348, M13349, M13350, M13351 Genomic DNA. Translation: AAA40444.1.
X14489 mRNA. Translation: CAA32651.1.
CCDSiCCDS19154.1.
PIRiA26323. YXMST.
RefSeqiNP_067263.1. NM_021288.4.
UniGeneiMm.268395.

Genome annotation databases

EnsembliENSMUST00000026846; ENSMUSP00000026846; ENSMUSG00000025747.
GeneIDi22171.
KEGGimmu:22171.
UCSCiuc008wux.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13019 mRNA. Translation: AAA40439.1.
M13352
, J02617, M13347, M13348, M13349, M13350, M13351 Genomic DNA. Translation: AAA40444.1.
X14489 mRNA. Translation: CAA32651.1.
CCDSiCCDS19154.1.
PIRiA26323. YXMST.
RefSeqiNP_067263.1. NM_021288.4.
UniGeneiMm.268395.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IHIX-ray1.94A/B1-307[»]
4E5OX-ray1.70A/B/C/D/E/F1-307[»]
4EB4X-ray1.74A/B/C/D1-307[»]
4EINX-ray1.75A/B1-307[»]
4EZ8X-ray1.17A1-307[»]
ProteinModelPortaliP07607.
SMRiP07607. Positions 21-307.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP07607.
ChEMBLiCHEMBL3160.
GuidetoPHARMACOLOGYi2642.

PTM databases

PhosphoSiteiP07607.

2D gel databases

REPRODUCTION-2DPAGEP07607.

Proteomic databases

MaxQBiP07607.
PaxDbiP07607.
PRIDEiP07607.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026846; ENSMUSP00000026846; ENSMUSG00000025747.
GeneIDi22171.
KEGGimmu:22171.
UCSCiuc008wux.2. mouse.

Organism-specific databases

CTDi7298.
MGIiMGI:98878. Tyms.

Phylogenomic databases

eggNOGiCOG0207.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP07607.
KOiK00560.
OMAiNEWADEN.
PhylomeDBiP07607.
TreeFamiTF353027.

Enzyme and pathway databases

UniPathwayiUPA00575.
ReactomeiREACT_198608. G1/S-Specific Transcription.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_238763. Pyrimidine biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP07607.
NextBioi302116.
PROiP07607.
SOURCEiSearch...

Gene expression databases

BgeeiP07607.
CleanExiMM_TYMS.
ExpressionAtlasiP07607. baseline and differential.
GenevestigatoriP07607.

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

  1. "Sequence of a cDNA for mouse thymidylate synthase reveals striking similarity with the prokaryotic enzyme."
    Perryman S.M., Rossana C., Deng T., Vanin E.F., Johnson L.F.
    Mol. Biol. Evol. 3:313-321(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the gene for mouse thymidylate synthase. Locations of introns and multiple transcriptional start sites."
    Deng T., Li D., Jenh C.-H., Johnson L.F.
    J. Biol. Chem. 261:16000-16005(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Thymidylate synthase gene expression is stimulated by some (but not all) introns."
    Deng T., Li Y., Johnson L.F.
    Nucleic Acids Res. 17:645-658(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 236-265.

Entry informationi

Entry nameiTYSY_MOUSE
AccessioniPrimary (citable) accession number: P07607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 4, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.