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Protein

Thymidylate synthase

Gene

Tyms

Organism
Rattus norvegicus (Rat)
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: 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)DescriptionActionsGraphical viewLength
Binding sitei44dUMPBy similarity1
Active sitei189NucleophileBy similarity1
Binding sitei2125,10-methylenetetrahydrofolateBy similarity1
Binding sitei220dUMPBy similarity1
Binding sitei3065,10-methylenetetrahydrofolate; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 170dUMP; shared with dimeric partnerBy similarity2
Nucleotide bindingi209 – 212dUMPBy similarity4
Nucleotide bindingi250 – 252dUMPBy similarity3

GO - Molecular functioni

  • cofactor binding Source: RGD
  • drug binding Source: RGD
  • folic acid binding Source: RGD
  • mRNA binding Source: RGD
  • nucleotide binding Source: RGD
  • protein homodimerization activity Source: RGD
  • sequence-specific mRNA binding Source: Ensembl
  • thymidylate synthase activity Source: RGD
  • translation repressor activity, nucleic acid binding Source: Ensembl

GO - Biological processi

  • aging Source: RGD
  • cartilage development Source: RGD
  • circadian rhythm Source: RGD
  • developmental growth Source: RGD
  • dTMP biosynthetic process Source: RGD
  • dTTP biosynthetic process Source: UniProtKB-UniPathway
  • dUMP metabolic process Source: RGD
  • immortalization of host cell by virus Source: RGD
  • intestinal epithelial cell maturation Source: RGD
  • liver regeneration Source: RGD
  • pyrimidine nucleobase metabolic process Source: RGD
  • regulation of translation Source: RGD
  • response to cytokine Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to folic acid Source: RGD
  • response to glucocorticoid Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organophosphorus Source: Ensembl
  • response to progesterone Source: RGD
  • response to toxic substance Source: RGD
  • response to vitamin A Source: RGD
  • tetrahydrofolate interconversion Source: Ensembl
  • tetrahydrofolate metabolic process Source: RGD
  • uracil metabolic process Source: RGD

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processNucleotide biosynthesis

Enzyme and pathway databases

ReactomeiR-RNO-499943. Interconversion of nucleotide di- and triphosphates.
SABIO-RKiP45352.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase (EC:2.1.1.45)
Short name:
TS
Short name:
TSase
Gene namesi
Name:Tyms
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi3921. Tyms.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4341.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409031 – 307Thymidylate synthaseAdd BLAST307

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei108PhosphoserineBy similarity1
Cross-linki286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP45352.
PRIDEiP45352.

PTM databases

PhosphoSitePlusiP45352.

Expressioni

Gene expression databases

BgeeiENSRNOG00000037225.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000053086.

Chemistry databases

BindingDBiP45352.

Structurei

Secondary structure

1307
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 37Combined sources14
Beta strandi39 – 41Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi49 – 60Combined sources12
Beta strandi69 – 71Combined sources3
Helixi75 – 86Combined sources12
Helixi93 – 96Combined sources4
Turni97 – 99Combined sources3
Turni102 – 104Combined sources3
Helixi105 – 107Combined sources3
Helixi109 – 114Combined sources6
Beta strandi118 – 120Combined sources3
Helixi129 – 134Combined sources6
Helixi154 – 164Combined sources11
Beta strandi172 – 174Combined sources3
Turni178 – 180Combined sources3
Helixi181 – 183Combined sources3
Beta strandi189 – 198Combined sources10
Beta strandi201 – 212Combined sources12
Turni213 – 215Combined sources3
Helixi216 – 235Combined sources20
Beta strandi238 – 252Combined sources15
Helixi253 – 255Combined sources3
Helixi256 – 264Combined sources9
Beta strandi272 – 275Combined sources4
Helixi282 – 284Combined sources3
Helixi287 – 289Combined sources3
Beta strandi290 – 293Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RTSX-ray3.30A/B1-307[»]
2TSRX-ray2.60A/B/C/D1-307[»]
ProteinModelPortaliP45352.
SMRiP45352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45352.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate synthase family.Curated

Phylogenomic databases

eggNOGiKOG0673. Eukaryota.
COG0207. LUCA.
GeneTreeiENSGT00390000014786.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP45352.
KOiK00560.
OMAiKQYLDLC.
OrthoDBiEOG091G0CV0.
PhylomeDBiP45352.
TreeFamiTF353027.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact. 1 hit.
InterProiView protein in InterPro
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
PfamiView protein in Pfam
PF00303. Thymidylat_synt. 1 hit.
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 1 hit.
PROSITEiView protein in PROSITE
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P45352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVEGSELQS GAQQPRTEAP QHGELQYLRQ VEHIMRCGFK KEDRTGTGTL
60 70 80 90 100
SVFGMQARYS LRDEFPLLTT KRVFWKGVLE ELLWFIKGST NAKELSSKGV
110 120 130 140 150
RIWDANGSRD FLDSLGFSAR QEGDLGPVYG FQWRHFGADY 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 PKLRILRKVE TIDDFKVEDF QIEGYNPHPT

IKMEMAV
Length:307
Mass (Da):35,017
Last modified:November 1, 1995 - v1
Checksum:i159F564D347B2B52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12138 mRNA. Translation: AAA92340.1.
BC126093 mRNA. Translation: AAI26094.1.
PIRiS53715.
RefSeqiNP_062052.1. NM_019179.1.
UniGeneiRn.162284.

Genome annotation databases

EnsembliENSRNOT00000056243; ENSRNOP00000053086; ENSRNOG00000037225.
GeneIDi29261.
KEGGirno:29261.

Similar proteinsi

Entry informationi

Entry nameiTYSY_RAT
AccessioniPrimary (citable) accession number: P45352
Secondary accession number(s): A0JN23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: August 30, 2017
This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families