Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P45352

- TYSY_RAT

UniProt

P45352 - TYSY_RAT

Protein

Thymidylate synthase

Gene

Tyms

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.

    P45352-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVEGSELQS GAQQPRTEAP QHGELQYLRQ VEHIMRCGFK KEDRTGTGTL    50
    SVFGMQARYS LRDEFPLLTT KRVFWKGVLE ELLWFIKGST NAKELSSKGV 100
    RIWDANGSRD FLDSLGFSAR QEGDLGPVYG FQWRHFGADY KDMDSDYSGQ 150
    GVDQLQKVID TIKTNPDDRR IIMCAWNPKD LPLMALPPCH ALCQFYVVNG 200
    ELSCQLYQRS GDMGLGVPFN IASYALLTYM IAHITGLQPG DFVHTLGDAH 250
    IYLNHIEPLK IQLQREPRPF PKLRILRKVE TIDDFKVEDF QIEGYNPHPT 300
    IKMEMAV 307
    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

    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