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Protein

Thymidylate synthase

Gene

TYMS

Organism
Homo sapiens (Human)
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.1 Publication

Catalytic activityi

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

Pathway:idTTP 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei195 – 1951

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS11096-MONOMER.
BRENDAi2.1.1.45. 2681.
ReactomeiREACT_21376. Pyrimidine biosynthesis.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
SABIO-RKP04818.
UniPathwayiUPA00575.

Protein family/group databases

MoonProtiP04818.

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 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:12441. TYMS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleolus Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti240839. 5-fluorouracil toxicity.
PharmGKBiPA359.

Chemistry

DrugBankiDB01101. Capecitabine.
DB00322. Floxuridine.
DB00544. Fluorouracil.
DB00441. Gemcitabine.
DB00650. Leucovorin.
DB00563. Methotrexate.
DB00642. Pemetrexed.
DB06813. Pralatrexate.
DB00293. Raltitrexed.
DB00432. Trifluridine.
DB00440. Trimethoprim.

Polymorphism and mutation databases

BioMutaiTYMS.
DMDMi136611.

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

BgeeiP04818.
CleanExiHS_TYMS.
ExpressionAtlasiP04818. baseline and differential.
GenevisibleiP04818. HS.

Organism-specific databases

HPAiCAB002784.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi113149. 36 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 – 4314Combined sources
Beta strandi45 – 484Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 6613Combined sources
Beta strandi68 – 703Combined sources
Turni75 – 784Combined sources
Helixi81 – 9212Combined sources
Helixi98 – 1014Combined sources
Turni103 – 1053Combined sources
Turni108 – 1103Combined sources
Helixi111 – 1133Combined sources
Helixi117 – 1204Combined sources
Helixi123 – 1275Combined sources
Turni132 – 1343Combined sources
Helixi136 – 1416Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi156 – 1583Combined sources
Helixi160 – 17011Combined sources
Beta strandi178 – 1814Combined sources
Helixi184 – 1863Combined sources
Turni187 – 1893Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi196 – 2049Combined sources
Beta strandi207 – 21812Combined sources
Turni219 – 2213Combined sources
Helixi222 – 24120Combined sources
Beta strandi244 – 25815Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 2687Combined sources
Beta strandi278 – 2814Combined sources
Helixi288 – 2903Combined sources
Helixi293 – 2953Combined sources
Beta strandi296 – 3005Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4JEFX-ray2.31A26-311[»]
4KPWX-ray2.03A1-313[»]
4O1UX-ray2.26A/B1-313[»]
4O1XX-ray2.32A/B/C/D1-313[»]
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.
GeneTreeiENSGT00390000014786.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP04818.
KOiK00560.
OMAiNEWADEN.
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. AlignAdd to basket

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

        10         20         30         40         50
MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR
60 70 80 90 100
TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE
110 120 130 140 150
LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME
160 170 180 190 200
SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ
210 220 230 240 250
FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH
260 270 280 290 300
TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG
310
YNPHPTIKME MAV
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:
EMBLi
GenBanki
DDBJi
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.
GeneIDi7298.
KEGGihsa:7298.
UCSCiuc010dka.1. human. [P04818-1]
uc010dkb.1. human.
uc010dkc.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4JEFX-ray2.31A26-311[»]
4KPWX-ray2.03A1-313[»]
4O1UX-ray2.26A/B1-313[»]
4O1XX-ray2.32A/B/C/D1-313[»]
DisProtiDP00073.
ProteinModelPortaliP04818.
SMRiP04818. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113149. 36 interactions.
IntActiP04818. 2 interactions.
MINTiMINT-2800458.
STRINGi9606.ENSP00000315644.

Chemistry

BindingDBiP04818.
ChEMBLiCHEMBL1952.
DrugBankiDB01101. Capecitabine.
DB00322. Floxuridine.
DB00544. Fluorouracil.
DB00441. Gemcitabine.
DB00650. Leucovorin.
DB00563. Methotrexate.
DB00642. Pemetrexed.
DB06813. Pralatrexate.
DB00293. Raltitrexed.
DB00432. Trifluridine.
DB00440. Trimethoprim.
GuidetoPHARMACOLOGYi2642.

Protein family/group databases

MoonProtiP04818.

PTM databases

PhosphoSiteiP04818.

Polymorphism and mutation databases

BioMutaiTYMS.
DMDMi136611.

Proteomic databases

MaxQBiP04818.
PaxDbiP04818.
PRIDEiP04818.

Protocols and materials databases

DNASUi7298.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7298.
GeneCardsiGC18P000657.
HGNCiHGNC:12441. TYMS.
HPAiCAB002784.
MIMi188350. gene.
neXtProtiNX_P04818.
Orphaneti240839. 5-fluorouracil toxicity.
PharmGKBiPA359.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0207.
GeneTreeiENSGT00390000014786.
HOGENOMiHOG000257899.
HOVERGENiHBG001934.
InParanoidiP04818.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG725DHX.
PhylomeDBiP04818.
TreeFamiTF353027.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciMetaCyc:HS11096-MONOMER.
BRENDAi2.1.1.45. 2681.
ReactomeiREACT_21376. Pyrimidine biosynthesis.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
SABIO-RKP04818.

Miscellaneous databases

ChiTaRSiTYMS. human.
EvolutionaryTraceiP04818.
GeneWikiiThymidylate_synthase.
GenomeRNAii7298.
NextBioi28543.
PROiP04818.
SOURCEiSearch...

Gene expression databases

BgeeiP04818.
CleanExiHS_TYMS.
ExpressionAtlasiP04818. baseline and differential.
GenevisibleiP04818. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.