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P45352

- TYSY_RAT

UniProt

P45352 - TYSY_RAT

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Protein

Thymidylate synthase

Gene

Tyms

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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: RGD
  2. drug binding Source: RGD
  3. folic acid binding Source: RGD
  4. mRNA binding Source: RGD
  5. nucleotide binding Source: RGD
  6. protein homodimerization activity Source: RGD
  7. thymidylate synthase activity Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

ReactomeiREACT_196414. G1/S-Specific Transcription.
REACT_212687. Pyrimidine biosynthesis.
SABIO-RKP45352.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi3921. 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: RGD
  5. nucleolus Source: RGD
  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_0000140903Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP45352.

PTM databases

PhosphoSiteiP45352.

Expressioni

Gene expression databases

GenevestigatoriP45352.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
307
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3714
Beta strandi39 – 413
Beta strandi44 – 463
Beta strandi49 – 6012
Beta strandi69 – 713
Helixi75 – 8612
Helixi93 – 964
Turni97 – 993
Turni102 – 1043
Helixi105 – 1073
Helixi109 – 1146
Beta strandi118 – 1203
Helixi129 – 1346
Helixi154 – 16411
Beta strandi172 – 1743
Turni178 – 1803
Helixi181 – 1833
Beta strandi189 – 19810
Beta strandi201 – 21212
Turni213 – 2153
Helixi216 – 23520
Beta strandi238 – 25215
Helixi253 – 2553
Helixi256 – 2649
Beta strandi272 – 2754
Helixi282 – 2843
Helixi287 – 2893
Beta strandi290 – 2934

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTSX-ray3.30A/B1-307[»]
2TSRX-ray2.60A/B/C/D1-307[»]
ProteinModelPortaliP45352.
SMRiP45352. Positions 21-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45352.

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidylate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0207.
GeneTreeiENSGT00390000014786.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP45352.
KOiK00560.
OMAiKWARSKE.
OrthoDBiEOG725DHX.
PhylomeDBiP45352.
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.

P45352 [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:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12138 mRNA. Translation: AAA92340.1 .
BC126093 mRNA. Translation: AAI26094.1 .
PIRi S53715.
RefSeqi NP_062052.1. NM_019179.1.
UniGenei Rn.162284.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RTS X-ray 3.30 A/B 1-307 [» ]
2TSR X-ray 2.60 A/B/C/D 1-307 [» ]
ProteinModelPortali P45352.
SMRi P45352. Positions 21-303.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P45352.
ChEMBLi CHEMBL4341.

PTM databases

PhosphoSitei P45352.

Proteomic databases

PRIDEi P45352.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000056243 ; ENSRNOP00000053086 ; ENSRNOG00000037225 .
GeneIDi 29261.
KEGGi rno:29261.

Organism-specific databases

CTDi 7298.
RGDi 3921. Tyms.

Phylogenomic databases

eggNOGi COG0207.
GeneTreei ENSGT00390000014786.
HOGENOMi HOG000257899.
HOVERGENi HBG001934.
InParanoidi P45352.
KOi K00560.
OMAi KWARSKE.
OrthoDBi EOG725DHX.
PhylomeDBi P45352.
TreeFami TF353027.

Enzyme and pathway databases

UniPathwayi UPA00575 .
Reactomei REACT_196414. G1/S-Specific Transcription.
REACT_212687. Pyrimidine biosynthesis.
SABIO-RK P45352.

Miscellaneous databases

EvolutionaryTracei P45352.
NextBioi 608588.
PROi P45352.

Gene expression databases

Genevestigatori P45352.

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
HAMAPi MF_00008. Thymidy_synth_bact.
InterProi IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view ]
Pfami PF00303. Thymidylat_synt. 1 hit.
[Graphical view ]
PRINTSi PR00108. THYMDSNTHASE.
SUPFAMi SSF55831. SSF55831. 1 hit.
TIGRFAMsi TIGR03284. thym_sym. 1 hit.
PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiTYSY_RAT
AccessioniPrimary (citable) accession number: P45352
Secondary accession number(s): A0JN23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 113 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. 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

External Data

Dasty 3