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P04818

- TYSY_HUMAN

UniProt

P04818 - TYSY_HUMAN

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Protein
Thymidylate synthase
Gene
TYMS, TS, OK/SW-cl.29
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

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
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB
  2. DNA replication Source: UniProtKB
  3. G1/S transition of mitotic cell cycle Source: Reactome
  4. aging Source: Ensembl
  5. cartilage development Source: Ensembl
  6. circadian rhythm Source: Ensembl
  7. dTMP biosynthetic process Source: Ensembl
  8. dTTP biosynthetic process Source: UniProtKB-UniPathway
  9. dUMP metabolic process Source: Ensembl
  10. deoxyribonucleoside monophosphate biosynthetic process Source: ProtInc
  11. developmental growth Source: Ensembl
  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
Complete GO annotation...

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. Cytoplasm. Mitochondrion. Mitochondrion matrix. 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
Complete GO annotation...

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 synthaseUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP04818.

Family & Domainsi

Sequence similaritiesi

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.
VSP_047745Add
BLAST
Alternative sequencei152 – 18534Missing in isoform 2.
VSP_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...

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

« 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: September 3, 2014
This is version 165 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

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