Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
2.1.1.45
Transferases;
Transferring one-carbon groups;
Methyltransferases;
thymidylate synthase
PDB | Resolution (Å) | PDB name |
---|---|---|
1HVY | 1.9 | Human thymidylate synthase complexed with dUMP and Raltitrexed, an antifolate drug, is in the closed conformation |
1HW3 | 2.0 | STRUCTURE OF HUMAN THYMIDYLATE SYNTHASE SUGGESTS ADVANTAGES OF CHEMOTHERAPY WITH NONCOMPETITIVE INHIBITORS |
1HW4 | 2.06 | STRUCTURE OF THYMIDYLATE SYNTHASE SUGGESTS ADVANTAGES OF CHEMOTHERAPY WITH NONCOMPETITIVE INHIBITORS |
1HZW | 2.0 | CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE SYNTHASE |
1I00 | 2.5 | CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE SYNTHASE, TERNARY COMPLEX WITH DUMP AND TOMUDEX |
1JU6 | 2.89 | Human Thymidylate Synthase Complex with dUMP and LY231514, A Pyrrolo(2,3-d)pyrimidine-based Antifolate |
1JUJ | 3.0 | Human Thymidylate Synthase Bound to dUMP and LY231514, a Pyrrolo(2,3-d)pyrimidine-based Antifolate |
1YPV | 1.8 | Structure of human thymidylate synthase at low salt conditions |
2ONB | 2.7 | Human Thymidylate Synthase at low salt conditions with PDPA bound |
2RD8 | 2.5 | Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195 |
2RDA | 2.67 | Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195 |
3EAW | 1.86 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3EBU | 2.05 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3ED7 | 1.56 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3EDW | 1.75 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3EF9 | 3.2 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3EGY | 2.18 | Crystal Structure of Human Thymidyalte Synthase A191K with Loop 181-197 stabilized in the inactive conformation |
3EHI | 2.0 | Crystal Structure of Human Thymidyalte Synthase M190K with Loop 181-197 stabilized in the inactive conformation |
3EJL | 3.2 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3GG5 | 2.77 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3GH0 | 1.56 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3GH2 | 1.75 | Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability |
3H9K | 2.65 | Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry |
3HB8 | 2.74 | Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry |
3N5E | 2.26 | Crystal Structure of human thymidylate synthase bound to a peptide inhibitor |
3N5G | 2.27 | Crystal Structure of histidine-tagged human thymidylate synthase |
3OB7 | 2.75 | Human Thymidylate Synthase R163K with Cys 195 covalently modified by Glutathione |
4E28 | 2.302 | Structure of human thymidylate synthase in inactive conformation with a novel non-peptidic inhibitor |
4FGT | 2.0 | Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive conformation of the enzyme. |
4G2O | 2.25 | Human Thymidylate Synthase M190K with bound Purpurogallin |
4G6W | 2.3 | Human Thymidylate Synthase M190K with bound 4-Bromobenzene-1,2,3-triol |
4GD7 | 2.29 | Wild-Type Human Thymidylate Synthase with bound Purpurogallin |
4GYH | 3.005 | Structure of human thymidylate synthase at high salt conditions |
4H1I | 3.095 | Structure of human thymidylate synthase at low salt conditions |
4JEF | 2.311 | Crystal structure of human thymidylate synthase Y202A in inactive conformation. |
4KPW | 2.03 | Crystal structure of His-tagged human thymidylate synthase R175A mutant |
4O1U | 2.26 | Crystal structure of human thymidylate synthase mutant Y202C |
4O1X | 2.32 | Crystal structure of human thymidylate synthase double mutant C195S-Y202C |
4UP1 | 2.991 | Crystal structure of native human Thymidylate synthase in active form |
5HS3 | 3.103 | Human thymidylate synthase complexed with dUMP and 3-amino-2-benzoyl-4-methylthieno[2,3-b]pyridin-6-ol |
5WRN | 2.39 | Human thymidylate synthase complexed with dCMP |
5X4W | 2.1 | Mutant human thymidylate synthase A191K crystallized in a sulfate-free condition |
5X4X | 2.31 | Mutant human thymidylate synthase A191K crystallized in a sulfate-containing condition |
5X4Y | 2.2 | Mutant human thymidylate synthase M190K crystallized in a sulfate-containing condition |
5X5A | 2.39 | Human thymidylate synthase bound with phosphate ion |
5X5D | 2.0 | Human thymidylate synthase bound with dUMP |
5X5Q | 2.79 | Human thymidylate synthase complexed with dUMP and raltitrexed |
5X66 | 1.99 | Human thymidylate synthase in complex with dUMP and methotrexate |
5X67 | 2.13 | Human thymidylate synthase in complex with dUMP and nolatrexed |
5X69 | 2.69 | Human thymidylate synthase with a fragment bound in the dimer interface |
6OJU | 2.884 | Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-D-glutamic acid |
6OJV | 2.593 | Crystal structure of human thymidylate synthase delta(7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid |
6PF3 | 2.391 | Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)-4-chlorobenzoic acid |
6PF4 | 2.854 | Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-(2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)phenyl)acetic acid |
6PF5 | 2.39 | Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-(2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)-4-methoxyphenyl)acetic acid |
6PF6 | 2.502 | Crystal structure of TS-DHFR from Cryptosporidium hominis in complex with NADPH, FdUMP and 2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)terephthalic acid |
6QXG | 2.08 | Crystal structure of His-tag human thymidylate synthase (HT-hTS) in complex with FdUMP |
6QXH | 2.04 | Crystal structure of His-tag human thymidylate synthase (HT-hTS) in complex with dUMP |
6QYQ | 2.25 | Crystal structure of human thymidylate synthase (hTS) variant R175C |
6R2E | 2.55 | Crystal structure of the human thymidylate synthase (hTS) interface variant Q62R |
6ZXO | 2.6 | Crystal structure of His-tagged human thymidylate synthase (HT-hTS) in complex with FdUMP and Raltitrexed (Tomudex) |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:0071897 | DNA biosynthetic process |
Biological Process | GO:0007568 | aging |
Biological Process | GO:0051216 | cartilage development |
Biological Process | GO:0007623 | circadian rhythm |
Biological Process | GO:0006231 | dTMP biosynthetic process |
Biological Process | GO:0006235 | dTTP biosynthetic process |
Biological Process | GO:0048589 | developmental growth |
Biological Process | GO:0060574 | intestinal epithelial cell maturation |
Biological Process | GO:0097421 | liver regeneration |
Biological Process | GO:0032259 | methylation |
Biological Process | GO:0017148 | negative regulation of translation |
Biological Process | GO:0034097 | response to cytokine |
Biological Process | GO:0045471 | response to ethanol |
Biological Process | GO:0051593 | response to folic acid |
Biological Process | GO:0051384 | response to glucocorticoid |
Biological Process | GO:0046683 | response to organophosphorus |
Biological Process | GO:0032570 | response to progesterone |
Biological Process | GO:0009636 | response to toxic substance |
Biological Process | GO:0033189 | response to vitamin A |
Biological Process | GO:0009410 | response to xenobiotic stimulus |
Biological Process | GO:0035999 | tetrahydrofolate interconversion |
Biological Process | GO:0019860 | uracil metabolic process |
Molecular Function | GO:0005542 | folic acid binding |
Molecular Function | GO:0000900 | mRNA regulatory element binding translation repressor activity |
Molecular Function | GO:0042803 | protein homodimerization activity |
Molecular Function | GO:1990825 | sequence-specific mRNA binding |
Molecular Function | GO:0004799 | thymidylate synthase activity |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0005743 | mitochondrial inner membrane |
Cellular Component | GO:0005759 | mitochondrial matrix |
Cellular Component | GO:0005739 | mitochondrion |
Cellular Component | GO:0005730 | nucleolus |
Cellular Component | GO:0005634 | nucleus |
InterPro | InterPro name |
---|---|
IPR000398 | Thymidylate synthase |
IPR020940 | Thymidylate synthase, active site |
IPR023451 | Thymidylate synthase/dCMP hydroxymethylase domain |
IPR036926 | Thymidylate synthase/dCMP hydroxymethylase superfamily |
IPR045097 | Thymidylate synthase/dCMP hydroxymethylase |
Pfam | Pfam name |
---|---|
PF00303 | Thymidylate synthase |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | Leaf | R-HSA-1430728 | Metabolism |
R-HSA-69205 | G1/S-Specific Transcription | Leaf | R-HSA-1640170 | Cell Cycle |
Location | ECO term | Pubmed |
---|---|---|
Cytoplasm | ECO:0000269 | PubMed:21876188 |
Mitochondrion | ECO:0000269 | PubMed:21876188 |
Mitochondrion inner membrane | ECO:0000269 | PubMed:21876188 |
Mitochondrion matrix | ECO:0000269 | PubMed:21876188 |
Nucleus | ECO:0000269 | PubMed:21876188 |
HPO ID | HPO name |
---|---|
HP:0000008 | Abnormal morphology of female internal genitalia |
HP:0000035 | Abnormal testis morphology |
HP:0000164 | Abnormality of the dentition |
HP:0000252 | Microcephaly |
HP:0000327 | Hypoplasia of the maxilla |
HP:0000365 | Hearing impairment |
HP:0000498 | Blepharitis |
HP:0000499 | Abnormal eyelash morphology |
HP:0000518 | Cataract |
HP:0000534 | Abnormal eyebrow morphology |
HP:0000600 | Abnormality of the pharynx |
HP:0000653 | Sparse eyelashes |
HP:0000668 | Hypodontia |
HP:0000670 | Carious teeth |
HP:0000679 | Taurodontia |
HP:0000704 | Periodontitis |
HP:0000819 | Diabetes mellitus |
HP:0000939 | Osteoporosis |
HP:0000975 | Hyperhidrosis |
HP:0000982 | Palmoplantar keratoderma |
HP:0001000 | Abnormality of skin pigmentation |
HP:0001018 | Abnormal palmar dermatoglyphics |
HP:0001034 | Hypermelanotic macule |
HP:0001053 | Hypopigmented skin patches |
HP:0001231 | Abnormal fingernail morphology |
HP:0001263 | Global developmental delay |
HP:0001394 | Cirrhosis |
HP:0001399 | Hepatic failure |
HP:0001488 | Bilateral ptosis |
HP:0001508 | Failure to thrive |
HP:0001511 | Intrauterine growth retardation |
HP:0001596 | Alopecia |
HP:0001744 | Splenomegaly |
HP:0001873 | Thrombocytopenia |
HP:0001874 | Abnormality of neutrophils |
HP:0001903 | Anemia |
HP:0001928 | Abnormality of coagulation |
HP:0002015 | Dysphagia |
HP:0002020 | Gastroesophageal reflux |
HP:0002024 | Malabsorption |
HP:0002205 | Recurrent respiratory infections |
HP:0002216 | Premature graying of hair |
HP:0002240 | Hepatomegaly |
HP:0002514 | Cerebral calcification |
HP:0002575 | Tracheoesophageal fistula |
HP:0002650 | Scoliosis |
HP:0002664 | Neoplasm |
HP:0002665 | Lymphoma |
HP:0002671 | Basal cell carcinoma |
HP:0002719 | Recurrent infections |
HP:0002720 | Decreased circulating IgA level |
HP:0002745 | Oral leukoplakia |
HP:0002757 | Recurrent fractures |
HP:0002850 | Decreased circulating total IgM |
HP:0002861 | Melanoma |
HP:0002894 | Neoplasm of the pancreas |
HP:0003577 | Congenital onset |
HP:0003593 | Infantile onset |
HP:0003621 | Juvenile onset |
HP:0004315 | Decreased circulating IgG level |
HP:0004322 | Short stature |
HP:0005374 | Cellular immunodeficiency |
HP:0005528 | Bone marrow hypocellularity |
HP:0006739 | Squamous cell carcinoma of the skin |
HP:0008065 | Aplasia/Hypoplasia of the skin |
HP:0008066 | Abnormal blistering of the skin |
HP:0008070 | Sparse hair |
HP:0008404 | Nail dystrophy |
HP:0008661 | Urethral stenosis |
HP:0008734 | Decreased testicular size |
HP:0009926 | Epiphora |
HP:0010450 | Esophageal stenosis |
HP:0010624 | Aplastic/hypoplastic toenail |
HP:0010885 | Avascular necrosis |
HP:0010984 | Digenic inheritance |
HP:0011364 | White hair |
HP:0012732 | Anorectal anomaly |
HP:0012733 | Macule |
HP:0031413 | Short telomere length |
HP:0100585 | Telangiectasia of the skin |
HP:0100627 | Displacement of the urethral meatus |
HP:0100670 | Coarse metaphyseal trabecularization |
HP:0200037 | Skin vesicle |
HP:0200042 | Skin ulcer |
Disease name | MONDO ID | ICD10 | ICD10 chapter | OMIM | Orphanet |
---|---|---|---|---|---|
dyskeratosis congenita, digenic | MONDO:0031057 | - | - | OMIM:620040 |