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P45352 (TYSY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 expression pattern PubMed 3471366. Source: RGD

cartilage development

Inferred from expression pattern PubMed 3471366. Source: RGD

circadian rhythm

Inferred from expression pattern PubMed 19628084. Source: RGD

dTMP biosynthetic process

Inferred from direct assay Ref.3. Source: RGD

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUMP metabolic process

Inferred from direct assay Ref.3. Source: RGD

developmental growth

Inferred from expression pattern PubMed 7471094. Source: RGD

immortalization of host cell by virus

Inferred from expression pattern PubMed 1247599. Source: RGD

intestinal epithelial cell maturation

Inferred from expression pattern PubMed 1260861. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 2707640. Source: RGD

pyrimidine nucleobase metabolic process

Inferred from expression pattern PubMed 9524100. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 10767379PubMed 9524100. Source: RGD

response to drug

Inferred from expression pattern PubMed 7686361. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 9305788. Source: RGD

response to folic acid

Inferred from expression pattern PubMed 9528665. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 2707640. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 9683817. Source: RGD

response to organophosphorus

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from expression pattern PubMed 9635926. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 8781506. Source: RGD

response to vitamin A

Inferred from expression pattern PubMed 10395942. Source: RGD

tetrahydrofolate metabolic process

Inferred from expression pattern PubMed 7503782. Source: RGD

uracil metabolic process

Inferred from expression pattern PubMed 2043679. Source: RGD

   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 direct assay PubMed 9148948. Source: RGD

nucleolus

Inferred from direct assay PubMed 9148948. Source: RGD

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncofactor binding

Inferred from direct assay Ref.3. Source: RGD

drug binding

Inferred from physical interaction Ref.3. Source: RGD

folic acid binding

Inferred from direct assay PubMed 7537805. Source: RGD

mRNA binding

Inferred from physical interaction PubMed 9891091. Source: RGD

nucleotide binding

Inferred from direct assay Ref.3. Source: RGD

protein homodimerization activity

Inferred from direct assay Ref.3. Source: RGD

thymidylate synthase activity

Inferred from direct assay Ref.3. Source: RGD

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_0000140903

Sites

Active site1891 By similarity

Amino acid modifications

Modified residue1081Phosphoserine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P45352 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 159F564D347B2B52

FASTA30735,017
        10         20         30         40         50         60 
MLVEGSELQS GAQQPRTEAP QHGELQYLRQ VEHIMRCGFK KEDRTGTGTL SVFGMQARYS 

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

       130        140        150        160        170        180 
QEGDLGPVYG FQWRHFGADY 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 PKLRILRKVE TIDDFKVEDF QIEGYNPHPT 


IKMEMAV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and expression of rat thymidylate synthase cDNA: phylogenetic comparison with human and mouse thymidylate synthases."
Ciesla J., Weiner K.X., Weiner R.S., Reston J.T., Maley G.F., Maley F.
Biochim. Biophys. Acta 1261:233-242(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Brain.
[3]"Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug."
Sotelo-Mundo R.R., Ciesla J., Dzik J.M., Rode W., Maley F., Maley G.F., Hardy L.W., Montfort W.R.
Biochemistry 38:1087-1094(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12138 mRNA. Translation: AAA92340.1.
BC126093 mRNA. Translation: AAI26094.1.
PIRS53715.
RefSeqNP_062052.1. NM_019179.1.
UniGeneRn.162284.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTSX-ray3.30A/B1-307[»]
2TSRX-ray2.60A/B/C/D1-307[»]
ProteinModelPortalP45352.
SMRP45352. Positions 21-303.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP45352.
ChEMBLCHEMBL4341.

PTM databases

PhosphoSiteP45352.

Proteomic databases

PRIDEP45352.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000056243; ENSRNOP00000053086; ENSRNOG00000037225.
GeneID29261.
KEGGrno:29261.

Organism-specific databases

CTD7298.
RGD3921. Tyms.

Phylogenomic databases

eggNOGCOG0207.
GeneTreeENSGT00390000014786.
HOGENOMHOG000257899.
HOVERGENHBG001934.
InParanoidP45352.
KOK00560.
OMAKWARSKE.
OrthoDBEOG725DHX.
PhylomeDBP45352.
TreeFamTF353027.

Enzyme and pathway databases

SABIO-RKP45352.
UniPathwayUPA00575.

Gene expression databases

GenevestigatorP45352.

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

EvolutionaryTraceP45352.
NextBio608588.
PROP45352.

Entry information

Entry nameTYSY_RAT
AccessionPrimary (citable) accession number: P45352
Secondary accession number(s): A0JN23
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 111 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