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P07607 (TYSY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidylate synthase

Short name=TS
Short name=TSase
EC=2.1.1.45
Gene names
Name:Tyms
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway By similarity. HAMAP-Rule MF_00008

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Subunit structure

Homodimer.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion matrix By similarity. Mitochondrion inner membrane By similarity HAMAP-Rule MF_00008.

Sequence similarities

Belongs to the thymidylate synthase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

dTMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUMP metabolic process

Inferred from electronic annotation. Source: Ensembl

developmental growth

Inferred from electronic annotation. Source: Ensembl

immortalization of host cell by virus

Inferred from electronic annotation. Source: Ensembl

intestinal epithelial cell maturation

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

polysaccharide metabolic process

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to organophosphorus

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

tetrahydrofolate metabolic process

Inferred from electronic annotation. Source: Ensembl

uracil metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncofactor binding

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from electronic annotation. Source: Ensembl

folic acid binding

Inferred from electronic annotation. Source: Ensembl

mRNA binding

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: Ensembl

thymidylate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 307306Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140902

Sites

Active site1891 By similarity

Amino acid modifications

Modified residue1081Phosphoserine By similarity

Secondary structure

................................................. 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07607 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: E4930618C487FD5E

FASTA30734,958
        10         20         30         40         50         60 
MLVVGSELQS DAQQLSAEAP RHGELQYLRQ VEHILRCGFK KEDRTGTGTL SVFGMQARYS 

        70         80         90        100        110        120 
LRDEFPLLTT KRVFWKGVLE ELLWFIKGST NAKELSSKGV RIWDANGSRD FLDSLGFSAR 

       130        140        150        160        170        180 
QEGDLGPVYG FQWRHFGAEY KDMDSDYSGQ GVDQLQKVID TIKTNPDDRR IIMCAWNPKD 

       190        200        210        220        230        240 
LPLMALPPCH ALCQFYVVNG ELSCQLYQRS GDMGLGVPFN IASYALLTYM IAHITGLQPG 

       250        260        270        280        290        300 
DFVHTLGDAH IYLNHIEPLK IQLQREPRPF PKLKILRKVE TIDDFKVEDF QIEGYNPHPT 


IKMEMAV 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13019 mRNA. Translation: AAA40439.1.
M13352 expand/collapse EMBL AC list , J02617, M13347, M13348, M13349, M13350, M13351 Genomic DNA. Translation: AAA40444.1.
X14489 mRNA. Translation: CAA32651.1.
PIRYXMST. A26323.
RefSeqNP_067263.1. NM_021288.4.
UniGeneMm.268395.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP07607.
SMRP07607. Positions 21-307.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP07607.
ChEMBLCHEMBL3160.

PTM databases

PhosphoSiteP07607.

2D gel databases

REPRODUCTION-2DPAGEP07607.

Proteomic databases

PaxDbP07607.
PRIDEP07607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026846; ENSMUSP00000026846; ENSMUSG00000025747.
GeneID22171.
KEGGmmu:22171.
UCSCuc008wux.2. mouse.

Organism-specific databases

CTD7298.
MGIMGI:98878. Tyms.

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257899.
HOVERGENHBG001934.
InParanoidP07607.
KOK00560.
OMANLGPVYG.
PhylomeDBP07607.
TreeFamTF353027.

Enzyme and pathway databases

UniPathwayUPA00575.

Gene expression databases

ArrayExpressP07607.
BgeeP07607.
CleanExMM_TYMS.
GenevestigatorP07607.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07607.
NextBio302116.
PROP07607.
SOURCESearch...

Entry information

Entry nameTYSY_MOUSE
AccessionPrimary (citable) accession number: P07607
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot