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Thymidylate synthase (TS) (TSase) (EC 2.1.1.45)

 TYSY_HUMAN              Reviewed;         313 AA.
P04818; Q8WYK3; Q8WYK4;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 197.
RecName: Full=Thymidylate synthase;
Short=TS;
Short=TSase;
EC=2.1.1.45;
Name=TYMS; Synonyms=TS; ORFNames=OK/SW-cl.29;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2987839; DOI=10.1093/nar/13.6.2035;
Takeishi K., Kaneda S., Ayusawa D., Shimizu K., Gotoh O., Seno T.;
"Nucleotide sequence of a functional cDNA for human thymidylate
synthase.";
Nucleic Acids Res. 13:2035-2043(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2243092;
Kaneda S., Nalbantoglu J., Takeishi K., Shimizu K., Gotoh O., Seno T.,
Ayusawa D.;
"Structural and functional analysis of the human thymidylate synthase
gene.";
J. Biol. Chem. 265:20277-20284(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE
SPLICING.
PubMed=12706868; DOI=10.1016/S0304-3835(03)00005-3;
Hisatomi H., Tanemura H., Iizuka T., Katsumata K., Nagao K.,
Sumida H., Udagawa H., Hikiji K.;
"Differential alternative splicing expressions of thymidylate synthase
isoforms.";
Cancer Lett. 193:127-131(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE OF 1-68.
PubMed=2532645;
Takeishi K., Kaneda S., Ayusawa D., Shimizu K., Gotoh O., Seno T.;
"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.";
J. Biochem. 106:575-583(1989).
[9]
PROTEIN SEQUENCE OF 2-25.
PubMed=3839505;
Shimizu K., Ayusawa D., Takeishi K., Seno T.;
"Purification and NH2-terminal amino acid sequence of human
thymidylate synthase in an overproducing transformant of mouse FM3A
cells.";
J. Biochem. 97:845-850(1985).
[10]
PROTEIN SEQUENCE OF 2-10.
PubMed=2656695;
Davisson V.J., Sirawaraporn W., Santi D.V.;
"Expression of human thymidylate synthase in Escherichia coli.";
J. Biol. Chem. 264:9145-9148(1989).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21876188; DOI=10.1073/pnas.1103623108;
Anderson D.D., Quintero C.M., Stover P.J.;
"Identification of a de novo thymidylate biosynthesis pathway in
mammalian mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287; LYS-292 AND LYS-308,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=8845352; DOI=10.1021/bi00050a007;
Schiffer C.A., Clifton I.J., Davisson V.J., Santi D.V., Stroud R.M.;
"Crystal structure of human thymidylate synthase: a structural
mechanism for guiding substrates into the active site.";
Biochemistry 34:16279-16287(1995).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=11329255; DOI=10.1021/bi002413i;
Phan J., Koli S., Minor W., Dunlap R.B., Berger S.H., Lebioda L.;
"Human thymidylate synthase is in the closed conformation when
complexed with dUMP and raltitrexed, an antifolate drug.";
Biochemistry 40:1897-1902(2001).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11278511; DOI=10.1074/jbc.M009493200;
Phan J., Steadman D.J., Koli S., Ding W.C., Minor W., Dunlap R.B.,
Berger S.H., Lebioda L.;
"Structure of human thymidylate synthase suggests advantages of
chemotherapy with noncompetitive inhibitors.";
J. Biol. Chem. 276:14170-14177(2001).
-!- FUNCTION: Contributes to the de novo mitochondrial thymidylate
biosynthesis pathway. {ECO:0000269|PubMed:21876188}.
-!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP =
dihydrofolate + dTMP.
-!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21876188}.
Cytoplasm {ECO:0000269|PubMed:21876188}. Mitochondrion
{ECO:0000269|PubMed:21876188}. Mitochondrion matrix
{ECO:0000269|PubMed:21876188}. Mitochondrion inner membrane
{ECO:0000269|PubMed:21876188}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P04818-1; Sequence=Displayed;
Name=2; Synonyms=delta4;
IsoId=P04818-2; Sequence=VSP_047746;
Note=Expressed both in normal and cancerous tissues.;
Name=3; Synonyms=delta2+3;
IsoId=P04818-3; Sequence=VSP_047745;
Note=Expressed only in cancerous tissues.;
-!- SIMILARITY: Belongs to the thymidylate synthase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=TYMS";
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EMBL; X02308; CAA26178.1; -; mRNA.
EMBL; D00596; BAA00472.1; -; Genomic_DNA.
EMBL; AB077207; BAB83676.1; -; mRNA.
EMBL; AB077208; BAB83677.1; -; mRNA.
EMBL; AB062290; BAB93473.1; -; mRNA.
EMBL; AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471113; EAX01716.1; -; Genomic_DNA.
EMBL; CH471113; EAX01720.1; -; Genomic_DNA.
EMBL; BC002567; AAH02567.1; -; mRNA.
EMBL; BC013919; AAH13919.1; -; mRNA.
EMBL; BC083512; AAH83512.1; -; mRNA.
EMBL; D00517; BAA00404.1; -; Genomic_DNA.
CCDS; CCDS11821.1; -. [P04818-1]
PIR; A23047; YXHUT.
RefSeq; NP_001062.1; NM_001071.2. [P04818-1]
UniGene; Hs.369762; -.
PDB; 1HVY; X-ray; 1.90 A; A/B/C/D=26-313.
PDB; 1HW3; X-ray; 2.00 A; A=1-313.
PDB; 1HW4; X-ray; 2.06 A; A=1-313.
PDB; 1HZW; X-ray; 2.00 A; A/B=1-313.
PDB; 1I00; X-ray; 2.50 A; A/B=1-313.
PDB; 1JU6; X-ray; 2.89 A; A/B/C/D=1-313.
PDB; 1JUJ; X-ray; 3.00 A; A/B/C/D=1-313.
PDB; 1YPV; X-ray; 1.80 A; A=1-313.
PDB; 2ONB; X-ray; 2.70 A; A=1-313.
PDB; 2RD8; X-ray; 2.50 A; A/B=1-313.
PDB; 2RDA; X-ray; 2.67 A; A/B/C/D/E/F=1-313.
PDB; 3EAW; X-ray; 1.86 A; X=1-313.
PDB; 3EBU; X-ray; 2.05 A; A=1-313.
PDB; 3ED7; X-ray; 1.56 A; A=26-313.
PDB; 3EDW; X-ray; 1.75 A; X=1-313.
PDB; 3EF9; X-ray; 3.20 A; A=1-313.
PDB; 3EGY; X-ray; 2.18 A; X=1-313.
PDB; 3EHI; X-ray; 2.00 A; X=1-313.
PDB; 3EJL; X-ray; 3.20 A; A/B/C/D=1-313.
PDB; 3GG5; X-ray; 2.77 A; A/B/C/D=1-313.
PDB; 3GH0; X-ray; 1.56 A; A=1-313.
PDB; 3GH2; X-ray; 1.75 A; X=1-313.
PDB; 3H9K; X-ray; 2.65 A; A/B/C/D/E=1-313.
PDB; 3HB8; X-ray; 2.74 A; A/B/C/D/E=1-313.
PDB; 3N5E; X-ray; 2.26 A; A/B=1-313.
PDB; 3N5G; X-ray; 2.27 A; A=1-313.
PDB; 3OB7; X-ray; 2.75 A; A/B/C/D/E=1-313.
PDB; 4E28; X-ray; 2.30 A; A=1-313.
PDB; 4FGT; X-ray; 2.00 A; A=1-311.
PDB; 4G2O; X-ray; 2.25 A; X=1-313.
PDB; 4G6W; X-ray; 2.30 A; X=1-313.
PDB; 4GD7; X-ray; 2.29 A; A=1-313.
PDB; 4GYH; X-ray; 3.00 A; A=1-313.
PDB; 4H1I; X-ray; 3.10 A; A/B/C/D=1-313.
PDB; 4JEF; X-ray; 2.31 A; A=26-311.
PDB; 4KPW; X-ray; 2.03 A; A=1-313.
PDB; 4O1U; X-ray; 2.26 A; A/B=1-313.
PDB; 4O1X; X-ray; 2.32 A; A/B/C/D=1-313.
PDB; 4UP1; X-ray; 2.99 A; A/B/C/D=1-313.
PDB; 5HS3; X-ray; 3.10 A; A/B/C/D/E/F=26-313.
PDB; 5WRN; X-ray; 2.39 A; A/B/C/D/E/F=26-313.
PDB; 5X4W; X-ray; 2.10 A; A=1-313.
PDB; 5X4X; X-ray; 2.31 A; A=1-313.
PDB; 5X4Y; X-ray; 2.20 A; A=1-313.
PDB; 5X5A; X-ray; 2.39 A; A/B/C/D/E/F=26-313.
PDB; 5X5D; X-ray; 2.00 A; A/B/C/D/E/F=26-313.
PDB; 5X5Q; X-ray; 2.79 A; A/B/C/D/E/F=26-313.
PDB; 5X66; X-ray; 1.99 A; A/B/C/D/E/F=26-313.
PDB; 5X67; X-ray; 2.13 A; A/B=26-313.
PDB; 5X69; X-ray; 2.69 A; A/B/C/D/E/F=26-313.
PDBsum; 1HVY; -.
PDBsum; 1HW3; -.
PDBsum; 1HW4; -.
PDBsum; 1HZW; -.
PDBsum; 1I00; -.
PDBsum; 1JU6; -.
PDBsum; 1JUJ; -.
PDBsum; 1YPV; -.
PDBsum; 2ONB; -.
PDBsum; 2RD8; -.
PDBsum; 2RDA; -.
PDBsum; 3EAW; -.
PDBsum; 3EBU; -.
PDBsum; 3ED7; -.
PDBsum; 3EDW; -.
PDBsum; 3EF9; -.
PDBsum; 3EGY; -.
PDBsum; 3EHI; -.
PDBsum; 3EJL; -.
PDBsum; 3GG5; -.
PDBsum; 3GH0; -.
PDBsum; 3GH2; -.
PDBsum; 3H9K; -.
PDBsum; 3HB8; -.
PDBsum; 3N5E; -.
PDBsum; 3N5G; -.
PDBsum; 3OB7; -.
PDBsum; 4E28; -.
PDBsum; 4FGT; -.
PDBsum; 4G2O; -.
PDBsum; 4G6W; -.
PDBsum; 4GD7; -.
PDBsum; 4GYH; -.
PDBsum; 4H1I; -.
PDBsum; 4JEF; -.
PDBsum; 4KPW; -.
PDBsum; 4O1U; -.
PDBsum; 4O1X; -.
PDBsum; 4UP1; -.
PDBsum; 5HS3; -.
PDBsum; 5WRN; -.
PDBsum; 5X4W; -.
PDBsum; 5X4X; -.
PDBsum; 5X4Y; -.
PDBsum; 5X5A; -.
PDBsum; 5X5D; -.
PDBsum; 5X5Q; -.
PDBsum; 5X66; -.
PDBsum; 5X67; -.
PDBsum; 5X69; -.
DisProt; DP00073; -.
ProteinModelPortal; P04818; -.
SMR; P04818; -.
BioGrid; 113149; 55.
IntAct; P04818; 9.
MINT; MINT-2800458; -.
STRING; 9606.ENSP00000315644; -.
BindingDB; P04818; -.
ChEMBL; CHEMBL1952; -.
DrugBank; DB03800; 2'-deoxyuridylic acid.
DrugBank; DB05308; ANX-510.
DrugBank; DB01101; Capecitabine.
DrugBank; DB00322; Floxuridine.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00441; Gemcitabine.
DrugBank; DB00563; Methotrexate.
DrugBank; DB08478; N-[2-chloro-5-(trifluoromethyl)phenyl]imidodicarbonimidic diamide.
DrugBank; DB05116; NB1011.
DrugBank; DB05457; OSI-7904L.
DrugBank; DB00642; Pemetrexed.
DrugBank; DB06813; Pralatrexate.
DrugBank; DB00293; Raltitrexed.
DrugBank; DB01643; Thymidine-5'-Phosphate.
DrugBank; DB00432; Trifluridine.
DrugBank; DB00440; Trimethoprim.
GuidetoPHARMACOLOGY; 2642; -.
MoonProt; P04818; -.
iPTMnet; P04818; -.
PhosphoSitePlus; P04818; -.
BioMuta; TYMS; -.
DMDM; 136611; -.
EPD; P04818; -.
PaxDb; P04818; -.
PeptideAtlas; P04818; -.
PRIDE; P04818; -.
TopDownProteomics; P04818-1; -. [P04818-1]
DNASU; 7298; -.
Ensembl; ENST00000323224; ENSP00000314727; ENSG00000176890. [P04818-2]
Ensembl; ENST00000323250; ENSP00000314902; ENSG00000176890. [P04818-3]
Ensembl; ENST00000323274; ENSP00000315644; ENSG00000176890. [P04818-1]
GeneID; 7298; -.
KEGG; hsa:7298; -.
UCSC; uc010dkb.2; human. [P04818-1]
CTD; 7298; -.
DisGeNET; 7298; -.
EuPathDB; HostDB:ENSG00000176890.15; -.
GeneCards; TYMS; -.
HGNC; HGNC:12441; TYMS.
HPA; CAB002784; -.
MalaCards; TYMS; -.
MIM; 188350; gene.
neXtProt; NX_P04818; -.
OpenTargets; ENSG00000176890; -.
Orphanet; 240839; 5-fluorouracil toxicity.
PharmGKB; PA359; -.
eggNOG; KOG0673; Eukaryota.
eggNOG; COG0207; LUCA.
GeneTree; ENSGT00390000014786; -.
HOGENOM; HOG000257899; -.
HOVERGEN; HBG001934; -.
InParanoid; P04818; -.
KO; K00560; -.
OMA; KQYLDLC; -.
OrthoDB; EOG091G0CV0; -.
PhylomeDB; P04818; -.
TreeFam; TF353027; -.
BioCyc; MetaCyc:HS11096-MONOMER; -.
BRENDA; 2.1.1.45; 2681.
Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
SABIO-RK; P04818; -.
SIGNOR; P04818; -.
UniPathway; UPA00575; -.
ChiTaRS; TYMS; human.
EvolutionaryTrace; P04818; -.
GeneWiki; Thymidylate_synthase; -.
GenomeRNAi; 7298; -.
PRO; PR:P04818; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000176890; -.
CleanEx; HS_TYMS; -.
ExpressionAtlas; P04818; baseline and differential.
Genevisible; P04818; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048037; F:cofactor binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0005542; F:folic acid binding; IC:BHF-UCL.
GO; GO:0000166; F:nucleotide binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:CAFA.
GO; GO:0004799; F:thymidylate synthase activity; IDA:CAFA.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:CAFA.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0071897; P:DNA biosynthetic process; IC:BHF-UCL.
GO; GO:0006231; P:dTMP biosynthetic process; IDA:CAFA.
GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0046078; P:dUMP metabolic process; IEA:Ensembl.
GO; GO:0019088; P:immortalization of host cell by virus; IEA:Ensembl.
GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; IDA:CAFA.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0046683; P:response to organophosphorus; IEP:UniProtKB.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL.
GO; GO:0019860; P:uracil metabolic process; IEA:Ensembl.
CDD; cd00351; TS_Pyrimidine_HMase; 1.
Gene3D; 3.30.572.10; -; 1.
HAMAP; MF_00008; Thymidy_synth_bact; 1.
InterPro; IPR023451; Thymidate_synth/dCMP_Mease.
InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
InterPro; IPR000398; Thymidylate_synthase.
InterPro; IPR020940; Thymidylate_synthase_AS.
Pfam; PF00303; Thymidylat_synt; 1.
PRINTS; PR00108; THYMDSNTHASE.
SUPFAM; SSF55831; SSF55831; 1.
TIGRFAMs; TIGR03284; thym_sym; 1.
PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Membrane;
Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
Nucleotide biosynthesis; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2656695,
ECO:0000269|PubMed:3839505}.
CHAIN 2 313 Thymidylate synthase.
/FTId=PRO_0000140901.
NP_BIND 175 176 dUMP; shared with dimeric partner.
{ECO:0000250|UniProtKB:P0A884}.
NP_BIND 215 218 dUMP. {ECO:0000250|UniProtKB:P0A884}.
NP_BIND 256 258 dUMP. {ECO:0000250|UniProtKB:P0A884}.
ACT_SITE 195 195 Nucleophile.
{ECO:0000250|UniProtKB:P0A884}.
BINDING 50 50 dUMP. {ECO:0000250|UniProtKB:P0A884}.
BINDING 218 218 5,10-methylenetetrahydrofolate.
{ECO:0000250|UniProtKB:P0A884}.
BINDING 226 226 dUMP. {ECO:0000250|UniProtKB:P0A884}.
BINDING 312 312 5,10-methylenetetrahydrofolate; via
carbonyl oxygen.
{ECO:0000250|UniProtKB:P0A884}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
CROSSLNK 287 287 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 292 292 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 308 308 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 69 151 Missing (in isoform 3).
{ECO:0000303|PubMed:12706868}.
/FTId=VSP_047745.
VAR_SEQ 152 185 Missing (in isoform 2).
{ECO:0000303|PubMed:12706868}.
/FTId=VSP_047746.
HELIX 30 43 {ECO:0000244|PDB:3ED7}.
STRAND 45 48 {ECO:0000244|PDB:3ED7}.
STRAND 50 52 {ECO:0000244|PDB:1YPV}.
STRAND 54 66 {ECO:0000244|PDB:3ED7}.
STRAND 68 70 {ECO:0000244|PDB:3EBU}.
TURN 75 78 {ECO:0000244|PDB:3ED7}.
HELIX 81 92 {ECO:0000244|PDB:3ED7}.
HELIX 98 101 {ECO:0000244|PDB:3ED7}.
TURN 103 105 {ECO:0000244|PDB:1HVY}.
TURN 108 110 {ECO:0000244|PDB:1HZW}.
HELIX 111 113 {ECO:0000244|PDB:1HVY}.
HELIX 117 120 {ECO:0000244|PDB:3ED7}.
HELIX 123 127 {ECO:0000244|PDB:3ED7}.
TURN 132 134 {ECO:0000244|PDB:4E28}.
HELIX 136 141 {ECO:0000244|PDB:3ED7}.
STRAND 149 151 {ECO:0000244|PDB:3ED7}.
STRAND 156 158 {ECO:0000244|PDB:3EHI}.
HELIX 160 170 {ECO:0000244|PDB:3ED7}.
STRAND 178 181 {ECO:0000244|PDB:3ED7}.
HELIX 184 186 {ECO:0000244|PDB:3ED7}.
TURN 187 189 {ECO:0000244|PDB:3ED7}.
STRAND 190 192 {ECO:0000244|PDB:3ED7}.
STRAND 196 204 {ECO:0000244|PDB:3ED7}.
STRAND 207 218 {ECO:0000244|PDB:3ED7}.
TURN 219 221 {ECO:0000244|PDB:3ED7}.
HELIX 222 241 {ECO:0000244|PDB:3ED7}.
STRAND 244 258 {ECO:0000244|PDB:3ED7}.
HELIX 259 261 {ECO:0000244|PDB:3ED7}.
HELIX 262 268 {ECO:0000244|PDB:3ED7}.
STRAND 278 281 {ECO:0000244|PDB:3ED7}.
HELIX 288 290 {ECO:0000244|PDB:3ED7}.
HELIX 293 295 {ECO:0000244|PDB:3ED7}.
STRAND 296 300 {ECO:0000244|PDB:3ED7}.
SEQUENCE 313 AA; 35716 MW; 148D377F19915B6A CRC64;
MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG
MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS
LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC
AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI
TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG
YNPHPTIKME MAV


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