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P04818

- TYSY_HUMAN

UniProt

P04818 - TYSY_HUMAN

Protein

Thymidylate synthase

Gene

TYMS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.1 Publication

    Catalytic activityi

    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei195 – 1951

    GO - Molecular functioni

    1. cofactor binding Source: Ensembl
    2. drug binding Source: Ensembl
    3. folic acid binding Source: Ensembl
    4. mRNA binding Source: Ensembl
    5. nucleotide binding Source: Ensembl
    6. thymidylate synthase activity Source: Reactome

    GO - Biological processi

    1. aging Source: Ensembl
    2. cartilage development Source: Ensembl
    3. circadian rhythm Source: Ensembl
    4. deoxyribonucleoside monophosphate biosynthetic process Source: ProtInc
    5. developmental growth Source: Ensembl
    6. DNA repair Source: UniProtKB
    7. DNA replication Source: UniProtKB
    8. dTMP biosynthetic process Source: Ensembl
    9. dTTP biosynthetic process Source: UniProtKB-UniPathway
    10. dUMP metabolic process Source: Ensembl
    11. G1/S transition of mitotic cell cycle Source: Reactome
    12. immortalization of host cell by virus Source: Ensembl
    13. intestinal epithelial cell maturation Source: Ensembl
    14. mitotic cell cycle Source: Reactome
    15. nucleobase-containing compound metabolic process Source: ProtInc
    16. nucleobase-containing small molecule metabolic process Source: Reactome
    17. organ regeneration Source: Ensembl
    18. phosphatidylinositol-mediated signaling Source: UniProtKB
    19. polysaccharide metabolic process Source: Ensembl
    20. pyrimidine nucleobase metabolic process Source: Reactome
    21. pyrimidine nucleoside biosynthetic process Source: Reactome
    22. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    23. response to cytokine Source: Ensembl
    24. response to drug Source: Ensembl
    25. response to ethanol Source: Ensembl
    26. response to folic acid Source: Ensembl
    27. response to glucocorticoid Source: Ensembl
    28. response to organophosphorus Source: UniProtKB
    29. response to progesterone Source: Ensembl
    30. response to toxic substance Source: Ensembl
    31. response to vitamin A Source: Ensembl
    32. small molecule metabolic process Source: Reactome
    33. tetrahydrofolate metabolic process Source: Ensembl
    34. uracil metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS11096-MONOMER.
    ReactomeiREACT_21376. Pyrimidine biosynthesis.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    SABIO-RKP04818.
    UniPathwayiUPA00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidylate synthase (EC:2.1.1.45)
    Short name:
    TS
    Short name:
    TSase
    Gene namesi
    Name:TYMS
    Synonyms:TS
    ORF Names:OK/SW-cl.29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:12441. TYMS.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Mitochondrion 1 Publication. Mitochondrion matrix 1 Publication. Mitochondrion inner membrane 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial matrix Source: UniProtKB
    5. mitochondrion Source: UniProtKB
    6. nucleolus Source: Ensembl
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti240839. 5-fluorouracil toxicity.
    240855. Capecitabine toxicity.
    240955. Susceptibility to adverse reaction due to 5-fluorouracil treatment.
    240963. Susceptibility to adverse reaction due to capecitabine treatment.
    PharmGKBiPA359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 313312Thymidylate synthasePRO_0000140901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP04818.
    PaxDbiP04818.
    PRIDEiP04818.

    PTM databases

    PhosphoSiteiP04818.

    Expressioni

    Gene expression databases

    ArrayExpressiP04818.
    BgeeiP04818.
    CleanExiHS_TYMS.
    GenevestigatoriP04818.

    Organism-specific databases

    HPAiCAB002784.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi113149. 38 interactions.
    IntActiP04818. 2 interactions.
    MINTiMINT-2800458.
    STRINGi9606.ENSP00000315644.

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 4314
    Beta strandi45 – 484
    Beta strandi50 – 523
    Beta strandi54 – 6613
    Beta strandi68 – 703
    Turni75 – 784
    Helixi81 – 9212
    Helixi98 – 1014
    Turni103 – 1053
    Turni108 – 1103
    Helixi111 – 1133
    Helixi117 – 1204
    Helixi123 – 1275
    Turni132 – 1343
    Helixi136 – 1416
    Beta strandi149 – 1513
    Beta strandi156 – 1583
    Helixi160 – 17011
    Beta strandi178 – 1814
    Helixi184 – 1863
    Turni187 – 1893
    Beta strandi190 – 1923
    Beta strandi196 – 2049
    Beta strandi207 – 21812
    Turni219 – 2213
    Helixi222 – 24120
    Beta strandi244 – 25815
    Helixi259 – 2613
    Helixi262 – 2687
    Beta strandi278 – 2814
    Helixi288 – 2903
    Helixi293 – 2953
    Beta strandi296 – 3005

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HVYX-ray1.90A/B/C/D26-313[»]
    1HW3X-ray2.00A1-313[»]
    1HW4X-ray2.06A1-313[»]
    1HZWX-ray2.00A/B1-313[»]
    1I00X-ray2.50A/B1-313[»]
    1JU6X-ray2.89A/B/C/D1-313[»]
    1JUJX-ray3.00A/B/C/D1-313[»]
    1YPVX-ray1.80A1-313[»]
    2ONBX-ray2.70A1-313[»]
    2RD8X-ray2.50A/B1-313[»]
    2RDAX-ray2.67A/B/C/D/E/F1-313[»]
    3EAWX-ray1.86X1-313[»]
    3EBUX-ray2.05A1-313[»]
    3ED7X-ray1.56A26-313[»]
    3EDWX-ray1.75X1-313[»]
    3EF9X-ray3.20A1-313[»]
    3EGYX-ray2.18X1-313[»]
    3EHIX-ray2.00X1-313[»]
    3EJLX-ray3.20A/B/C/D1-313[»]
    3GG5X-ray2.77A/B/C/D1-313[»]
    3GH0X-ray1.56A1-313[»]
    3GH2X-ray1.75X1-313[»]
    3H9KX-ray2.65A/B/C/D/E1-313[»]
    3HB8X-ray2.74A/B/C/D/E1-313[»]
    3N5EX-ray2.26A/B1-313[»]
    3N5GX-ray2.27A1-313[»]
    3OB7X-ray2.75A/B/C/D/E1-313[»]
    4E28X-ray2.30A1-313[»]
    4FGTX-ray2.00A1-311[»]
    4G2OX-ray2.25X1-313[»]
    4G6WX-ray2.30X1-313[»]
    4GD7X-ray2.29A1-313[»]
    4GYHX-ray3.00A1-313[»]
    4H1IX-ray3.10A/B/C/D1-313[»]
    4KPWX-ray2.03A1-313[»]
    DisProtiDP00073.
    ProteinModelPortaliP04818.
    SMRiP04818. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04818.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymidylate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0207.
    HOGENOMiHOG000257899.
    HOVERGENiHBG001934.
    InParanoidiP04818.
    KOiK00560.
    OMAiELLWIYQ.
    OrthoDBiEOG725DHX.
    PhylomeDBiP04818.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04818-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR    50
    TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE 100
    LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME 150
    SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ 200
    FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH 250
    TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG 300
    YNPHPTIKME MAV 313
    Length:313
    Mass (Da):35,716
    Last modified:January 23, 2007 - v3
    Checksum:i148D377F19915B6A
    GO
    Isoform 2 (identifier: P04818-2) [UniParc]FASTAAdd to Basket

    Also known as: delta4

    The sequence of this isoform differs from the canonical sequence as follows:
         152-185: Missing.

    Note: Expressed both in normal and cancerous tissues.

    Show »
    Length:279
    Mass (Da):31,759
    Checksum:i10B3A53DE10AB763
    GO
    Isoform 3 (identifier: P04818-3) [UniParc]FASTAAdd to Basket

    Also known as: delta2+3

    The sequence of this isoform differs from the canonical sequence as follows:
         69-151: Missing.

    Note: Expressed only in cancerous tissues.

    Show »
    Length:230
    Mass (Da):26,140
    Checksum:iD09F8316A504A02A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 15183Missing in isoform 3. 1 PublicationVSP_047745Add
    BLAST
    Alternative sequencei152 – 18534Missing in isoform 2. 1 PublicationVSP_047746Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02308 mRNA. Translation: CAA26178.1.
    D00596 Genomic DNA. Translation: BAA00472.1.
    AB077207 mRNA. Translation: BAB83676.1.
    AB077208 mRNA. Translation: BAB83677.1.
    AB062290 mRNA. Translation: BAB93473.1.
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01716.1.
    CH471113 Genomic DNA. Translation: EAX01720.1.
    BC002567 mRNA. Translation: AAH02567.1.
    BC013919 mRNA. Translation: AAH13919.1.
    BC083512 mRNA. Translation: AAH83512.1.
    D00517 Genomic DNA. Translation: BAA00404.1.
    CCDSiCCDS11821.1. [P04818-1]
    PIRiA23047. YXHUT.
    RefSeqiNP_001062.1. NM_001071.2. [P04818-1]
    UniGeneiHs.369762.

    Genome annotation databases

    EnsembliENST00000323224; ENSP00000314727; ENSG00000176890. [P04818-2]
    ENST00000323250; ENSP00000314902; ENSG00000176890. [P04818-3]
    ENST00000323274; ENSP00000315644; ENSG00000176890. [P04818-1]
    GeneIDi7298.
    KEGGihsa:7298.
    UCSCiuc010dka.1. human. [P04818-1]
    uc010dkb.1. human.
    uc010dkc.1. human.

    Polymorphism databases

    DMDMi136611.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02308 mRNA. Translation: CAA26178.1 .
    D00596 Genomic DNA. Translation: BAA00472.1 .
    AB077207 mRNA. Translation: BAB83676.1 .
    AB077208 mRNA. Translation: BAB83677.1 .
    AB062290 mRNA. Translation: BAB93473.1 .
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01716.1 .
    CH471113 Genomic DNA. Translation: EAX01720.1 .
    BC002567 mRNA. Translation: AAH02567.1 .
    BC013919 mRNA. Translation: AAH13919.1 .
    BC083512 mRNA. Translation: AAH83512.1 .
    D00517 Genomic DNA. Translation: BAA00404.1 .
    CCDSi CCDS11821.1. [P04818-1 ]
    PIRi A23047. YXHUT.
    RefSeqi NP_001062.1. NM_001071.2. [P04818-1 ]
    UniGenei Hs.369762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HVY X-ray 1.90 A/B/C/D 26-313 [» ]
    1HW3 X-ray 2.00 A 1-313 [» ]
    1HW4 X-ray 2.06 A 1-313 [» ]
    1HZW X-ray 2.00 A/B 1-313 [» ]
    1I00 X-ray 2.50 A/B 1-313 [» ]
    1JU6 X-ray 2.89 A/B/C/D 1-313 [» ]
    1JUJ X-ray 3.00 A/B/C/D 1-313 [» ]
    1YPV X-ray 1.80 A 1-313 [» ]
    2ONB X-ray 2.70 A 1-313 [» ]
    2RD8 X-ray 2.50 A/B 1-313 [» ]
    2RDA X-ray 2.67 A/B/C/D/E/F 1-313 [» ]
    3EAW X-ray 1.86 X 1-313 [» ]
    3EBU X-ray 2.05 A 1-313 [» ]
    3ED7 X-ray 1.56 A 26-313 [» ]
    3EDW X-ray 1.75 X 1-313 [» ]
    3EF9 X-ray 3.20 A 1-313 [» ]
    3EGY X-ray 2.18 X 1-313 [» ]
    3EHI X-ray 2.00 X 1-313 [» ]
    3EJL X-ray 3.20 A/B/C/D 1-313 [» ]
    3GG5 X-ray 2.77 A/B/C/D 1-313 [» ]
    3GH0 X-ray 1.56 A 1-313 [» ]
    3GH2 X-ray 1.75 X 1-313 [» ]
    3H9K X-ray 2.65 A/B/C/D/E 1-313 [» ]
    3HB8 X-ray 2.74 A/B/C/D/E 1-313 [» ]
    3N5E X-ray 2.26 A/B 1-313 [» ]
    3N5G X-ray 2.27 A 1-313 [» ]
    3OB7 X-ray 2.75 A/B/C/D/E 1-313 [» ]
    4E28 X-ray 2.30 A 1-313 [» ]
    4FGT X-ray 2.00 A 1-311 [» ]
    4G2O X-ray 2.25 X 1-313 [» ]
    4G6W X-ray 2.30 X 1-313 [» ]
    4GD7 X-ray 2.29 A 1-313 [» ]
    4GYH X-ray 3.00 A 1-313 [» ]
    4H1I X-ray 3.10 A/B/C/D 1-313 [» ]
    4KPW X-ray 2.03 A 1-313 [» ]
    DisProti DP00073.
    ProteinModelPortali P04818.
    SMRi P04818. Positions 1-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113149. 38 interactions.
    IntActi P04818. 2 interactions.
    MINTi MINT-2800458.
    STRINGi 9606.ENSP00000315644.

    Chemistry

    BindingDBi P04818.
    ChEMBLi CHEMBL1952.
    DrugBanki DB01101. Capecitabine.
    DB00322. Floxuridine.
    DB00544. Fluorouracil.
    DB00441. Gemcitabine.
    DB00650. Leucovorin.
    DB00642. Pemetrexed.
    DB00293. Raltitrexed.
    DB00432. Trifluridine.
    GuidetoPHARMACOLOGYi 2642.

    PTM databases

    PhosphoSitei P04818.

    Polymorphism databases

    DMDMi 136611.

    Proteomic databases

    MaxQBi P04818.
    PaxDbi P04818.
    PRIDEi P04818.

    Protocols and materials databases

    DNASUi 7298.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323224 ; ENSP00000314727 ; ENSG00000176890 . [P04818-2 ]
    ENST00000323250 ; ENSP00000314902 ; ENSG00000176890 . [P04818-3 ]
    ENST00000323274 ; ENSP00000315644 ; ENSG00000176890 . [P04818-1 ]
    GeneIDi 7298.
    KEGGi hsa:7298.
    UCSCi uc010dka.1. human. [P04818-1 ]
    uc010dkb.1. human.
    uc010dkc.1. human.

    Organism-specific databases

    CTDi 7298.
    GeneCardsi GC18P000657.
    HGNCi HGNC:12441. TYMS.
    HPAi CAB002784.
    MIMi 188350. gene.
    neXtProti NX_P04818.
    Orphaneti 240839. 5-fluorouracil toxicity.
    240855. Capecitabine toxicity.
    240955. Susceptibility to adverse reaction due to 5-fluorouracil treatment.
    240963. Susceptibility to adverse reaction due to capecitabine treatment.
    PharmGKBi PA359.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0207.
    HOGENOMi HOG000257899.
    HOVERGENi HBG001934.
    InParanoidi P04818.
    KOi K00560.
    OMAi ELLWIYQ.
    OrthoDBi EOG725DHX.
    PhylomeDBi P04818.
    TreeFami TF353027.

    Enzyme and pathway databases

    UniPathwayi UPA00575 .
    BioCyci MetaCyc:HS11096-MONOMER.
    Reactomei REACT_21376. Pyrimidine biosynthesis.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    SABIO-RK P04818.

    Miscellaneous databases

    ChiTaRSi TYMS. human.
    EvolutionaryTracei P04818.
    GeneWikii Thymidylate_synthase.
    GenomeRNAii 7298.
    NextBioi 28543.
    PROi P04818.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04818.
    Bgeei P04818.
    CleanExi HS_TYMS.
    Genevestigatori P04818.

    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. "Nucleotide sequence of a functional cDNA for human thymidylate synthase."
      Takeishi K., Kaneda S., Ayusawa D., Shimizu K., Gotoh O., Seno T.
      Nucleic Acids Res. 13:2035-2043(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structural and functional analysis of the human thymidylate synthase gene."
      Kaneda S., Nalbantoglu J., Takeishi K., Shimizu K., Gotoh O., Seno T., Ayusawa D.
      J. Biol. Chem. 265:20277-20284(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Differential alternative splicing expressions of thymidylate synthase isoforms."
      Hisatomi H., Tanemura H., Iizuka T., Katsumata K., Nagao K., Sumida H., Udagawa H., Hikiji K.
      Cancer Lett. 193:127-131(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
    4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Bone marrow, Placenta and Skin.
    8. "Human thymidylate synthase gene: isolation of phage clones which cover a functionally active gene and structural analysis of the region upstream from the translation initiation codon."
      Takeishi K., Kaneda S., Ayusawa D., Shimizu K., Gotoh O., Seno T.
      J. Biochem. 106:575-583(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-68.
    9. "Purification and NH2-terminal amino acid sequence of human thymidylate synthase in an overproducing transformant of mouse FM3A cells."
      Shimizu K., Ayusawa D., Takeishi K., Seno T.
      J. Biochem. 97:845-850(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25.
    10. "Expression of human thymidylate synthase in Escherichia coli."
      Davisson V.J., Sirawaraporn W., Santi D.V.
      J. Biol. Chem. 264:9145-9148(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria."
      Anderson D.D., Quintero C.M., Stover P.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site."
      Schiffer C.A., Clifton I.J., Davisson V.J., Santi D.V., Stroud R.M.
      Biochemistry 34:16279-16287(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    16. "Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug."
      Phan J., Koli S., Minor W., Dunlap R.B., Berger S.H., Lebioda L.
      Biochemistry 40:1897-1902(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    17. "Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors."
      Phan J., Steadman D.J., Koli S., Ding W.C., Minor W., Dunlap R.B., Berger S.H., Lebioda L.
      J. Biol. Chem. 276:14170-14177(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiTYSY_HUMAN
    AccessioniPrimary (citable) accession number: P04818
    Secondary accession number(s): Q8WYK3, Q8WYK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 166 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3