Thymidine phosphorylase
Details
- Name
- Thymidine phosphorylase
- Synonyms
- 2.4.2.4
- ECGF1
- Gliostatin
- PD-ECGF
- Platelet-derived endothelial cell growth factor
- TdRPase
- TP
- Gene Name
- TYMP
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0004303|Thymidine phosphorylase MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG VGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP QQ
- Number of residues
- 482
- Molecular Weight
- 49954.965
- Theoretical pI
- 5.19
- GO Classification
- Functionsphosphorylase activity / platelet-derived growth factor receptor binding / pyrimidine-nucleoside phosphorylase activity / thymidine phosphorylase activity / transferase activity, transferring pentosyl groupsProcessesangiogenesis / cell differentiation / chemotaxis / DNA replication / mitochondrial genome maintenance / nucleobase-containing small molecule metabolic process / pyrimidine nucleobase metabolic process / pyrimidine nucleoside catabolic process / pyrimidine nucleoside salvage / pyrimidine nucleotide metabolic process / small molecule metabolic processComponentscytosol
- General Function
- Transferase activity, transferring pentosyl groups
- Specific Function
- May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0020602|Thymidine phosphorylase (TYMP) ATGGCAGCCTTGATGACCCCGGGAACCGGGGCCCCACCCGCGCCTGGTGACTTCTCCGGG GAAGGGAGCCAGGGACTTCCCGACCCTTCGCCAGAGCCCAAGCAGCTCCCGGAGCTGATC CGCATGAAGCGAGACGGAGGCCGCCTGAGCGAAGCGGACATCAGGGGCTTCGTGGCCGCT GTGGTGAATGGGAGCGCGCAGGGCGCACAGATCGGGGCCATGCTGATGGCCATCCGACTT CGGGGCATGGATCTGGAGGAGACCTCGGTGCTGACCCAGGCCCTGGCTCAGTCGGGACAG CAGCTGGAGTGGCCAGAGGCCTGGCGCCAGCAGCTTGTGGACAAGCATTCCACAGGGGGT GTGGGTGACAAGGTCAGCCTGGTCCTCGCACCTGCCCTGGCGGCATGTGGCTGCAAGGTG CCAATGATCAGCGGACGTGGTCTGGGGCACACAGGAGGCACCTTGGATAAGCTGGAGTCT ATTCCTGGATTCAATGTCATCCAGAGCCCAGAGCAGATGCAAGTGCTGCTGGACCAGGCG GGCTGCTGTATCGTGGGTCAGAGTGAGCAGCTGGTTCCTGCGGACGGAATCCTATATGCA GCCAGAGATGTGACAGCCACCGTGGACAGCCTGCCACTCATCACAGCCTCCATTCTCAGT AAGAAACTCGTGGAGGGGCTGTCCGCTCTGGTGGTGGACGTTAAGTTCGGAGGGGCCGCC GTCTTCCCCAACCAGGAGCAGGCCCGGGAGCTGGCAAAGACGCTGGTTGGCGTGGGAGCC AGCCTAGGGCTTCGGGTCGCGGCAGCGCTGACCGCCATGGACAAGCCCCTGGGTCGCTGC GTGGGCCACGCCCTGGAGGTGGAGGAGGCGCTGCTCTGCATGGACGGCGCAGGCCCGCCA GACTTAAGGGACCTGGTCACCACGCTCGGGGGCGCCCTGCTCTGGCTCAGCGGACACGCG GGGACTCAGGCCCAGGGCGCTGCCCGGGTGGCCGCGGCGCTGGACGACGGCTCGGCCCTT GGCCGCTTCGAGCGGATGCTGGCGGCGCAGGGCGTGGATCCCGGTCTGGCCCGAGCCCTG TGCTCGGGAAGTCCCGCAGAACGCCGGCAGCTGCTGCCTCGCGCCCGGGAGCAGGAGGAG CTGCTGGCGCCCGCAGATGGCACCGTGGAGCTGGTCCGGGCGCTGCCGCTGGCGCTGGTG CTGCACGAGCTCGGGGCCGGGCGCAGCCGCGCTGGGGAGCCGCTCCGCCTGGGGGTGGGC GCAGAGCTGCTGGTCGACGTGGGTCAGAGGCTGCGCCGTGGGACCCCCTGGCTCCGCGTG CACCGGGACGGCCCCGCGCTCAGCGGCCCGCAGAGCCGCGCCCTGCAGGAGGCGCTCGTA CTCTCCGACCGCGCGCCATTCGCCGCCCCCTCGCCCTTCGCAGAGCTCGTTCTGCCGCCG CAGCAATAA
- Chromosome Location
- 22
- Locus
- 22q13|22q13.33
- External Identifiers
Resource Link UniProtKB ID P19971 UniProtKB Entry Name TYPH_HUMAN GenBank Protein ID 189701 GenBank Gene ID M63193 GenAtlas ID ECGF1 HGNC ID HGNC:3148 - General References
- Ishikawa F, Miyazono K, Hellman U, Drexler H, Wernstedt C, Hagiwara K, Usuki K, Takaku F, Risau W, Heldin CH: Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor. Nature. 1989 Apr 13;338(6216):557-62. [Article]
- Finnis C, Goodey A, Courtney M, Sleep D: Expression of recombinant platelet-derived endothelial cell growth factor in the yeast Saccharomyces cerevisiae. Yeast. 1992 Jan;8(1):57-60. [Article]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [Article]
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- Furukawa T, Yoshimura A, Sumizawa T, Haraguchi M, Akiyama S, Fukui K, Ishizawa M, Yamada Y: Angiogenic factor. Nature. 1992 Apr 23;356(6371):668. [Article]
- Asai K, Nakanishi K, Isobe I, Eksioglu YZ, Hirano A, Hama K, Miyamoto T, Kato T: Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. J Biol Chem. 1992 Oct 5;267(28):20311-6. [Article]
- Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH: Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Norman RA, Barry ST, Bate M, Breed J, Colls JG, Ernill RJ, Luke RW, Minshull CA, McAlister MS, McCall EJ, McMiken HH, Paterson DS, Timms D, Tucker JA, Pauptit RA: Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor. Structure. 2004 Jan;12(1):75-84. [Article]
- El Omari K, Bronckaers A, Liekens S, Perez-Perez MJ, Balzarini J, Stammers DK: Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implications for drug design. Biochem J. 2006 Oct 15;399(2):199-204. [Article]
- Mitsiki E, Papageorgiou AC, Iyer S, Thiyagarajan N, Prior SH, Sleep D, Finnis C, Acharya KR: Structures of native human thymidine phosphorylase and in complex with 5-iodouracil. Biochem Biophys Res Commun. 2009 Sep 4;386(4):666-70. doi: 10.1016/j.bbrc.2009.06.104. Epub 2009 Jun 23. [Article]
- Nishino I, Spinazzola A, Hirano M: Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science. 1999 Jan 29;283(5402):689-92. [Article]
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Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01101 Capecitabine approved, investigational no substrate Details DB00322 Floxuridine approved unknown substrate Details DB00544 Fluorouracil approved unknown substrate Details DB00432 Trifluridine approved, investigational unknown substrate Details DB00369 Cidofovir approved unknown inhibitor Details DB06433 Tezacitabine investigational unknown inducer Details DB09343 Tipiracil approved, investigational yes inhibitor Details