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TYMP (thymidine phosphorylase)

Written2010-03Irene V Bijnsdorp, Godefridus J Peters
Department of Medical Oncology, VU University Medical Center, Amsterdam, The Netherlands

(Note : for Links provided by Atlas : click)


HGNC Alias namegliostatin
HGNC Previous nameMNGIE
HGNC Previous nameendothelial cell growth factor 1 (platelet-derived)
LocusID (NCBI) 1890
Atlas_Id 40397
Location 22q13.33  [Link to chromosome band 22q13]
Location_base_pair Starts at 50525753 and ends at 50530012 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TYMP.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
LMF2 (22q13.33)::TYMP (22q13.33)TYMP (22q13.33)::PPP6R2 (22q13.33)


Note The TP gene encodes an angiogenic factor which promotes angiogenesis both in vitro and in vivo and is involved in nucleotide synthesis and thymidine phosphorolysis.
  TYMP is located on chromosome 22 of which 3 transcripts have been identified.
Description Thymidine phosphorylase is located at chromosome 22 in the region of q13.33. cDNA is approximately 1.8 kb long, consisting of 10 exons in a 4.3 kb region (Hagiwara et al., 1991; Stenman et al., 1992). TP was first cloned and sequenced in 1989 (Ishikawa et al., 1989). The nucleic acid sequence of TP is highly conserved, the human TP shares 39% sequence identity with that of E. coli (Barton et al., 1992).
Transcription The promoter region of the TP gene has no TATA box or CCAAT box, but has a high G-C content and seven copies of the SP-1 binding site upstream from the transcription start site. Exact TP gene regulation is unknown, but has been described to be (indirectly) regulated by NFkB, TNF-alpha and IFN-gamma (Waguri et al., 1997; Zhu et al., 2002; Zhu et al., 2003; Eda et al., 1993; de Bruin et al., 2004).


Note Thymidine phosphorylase was first identified as the platelet-derived endothelial cell growth factor, because it was related to endothelial cell growth (Miyazono et al., 1987; Ishikawa et al., 1989). Later on, it was found that it was identical to thymidine phosphorylase (Furukawa et al., 1992). Thymidine phosphorylase (TP) is the most correct name to refer to this protein, since it catalyzes the phopshorolysis of thymidine to thymine. TP undergoes limited post-translational modification and is not glycosylated. Covalent linkage between serine residues of TP and phosphate groups of nucleotides has been observed, which may facilitate secretion of the protein (Usuki et al., 1991). However, TP does not contain a classical secretion signal (Ishikawa et al., 1989). TP is a dimer, consisting of two identical subunits that are non-covalently associated (Desgranges et al., 1981) with its dimeric molecular mass ranging from 90 kD in Escherichia coli to 110 kD in mammals (Schwartz, 1978; Desgranges et al., 1981).
Description TP protein does not contain a known receptor binding region or a secretion signal (Ishikawa et al., 1989). It is implicated in nucleotide synthesis and degradation of thymidine. TP is also implicated in angiogenesis (reviewed in de Bruin et al., 2006; Liekens et al., 2007; Bronckaers et al., 2009).
Expression TP is highly expressed in liver tissues. Furthermore, TP is often overexpressed in tumor sites and is involved in inflammatory diseases, such as rheumatoid arthritis.
Localisation TP is expressed in the cytoplasm and the nucleus (Fox et al., 1995).
Function TP catalyzes the phosphorolysis of thymidine (TdR) to thymine and 2-deoxy-alpha-D-ribose 1-phosphate (dR-1-P). TP can also catalyze the formation of thymidine from thymine and dR-1-P. TP also catalyzes the phosphorolysis of deoxyuridine to uracil and dR-1-P. TP also has deoxyribosyl transferase activity by which the deoxyribosyl moiety is transferred from a pyrimidine nucleoside to another pyrimidine base. Subsequently a new pyrimidine nucleoside is formed.
The sugars that are formed by degradation of thymidine are thought to play a role in the induction of angiogenesis. Deoxyribose-1-P can be converted to deoxyribose-5-phosphate or degraded to deoxyribose. Deoxyribose can be secreted, and possibly attract endothelial cells to form new blood vessels (reviewed in de Bruin et al., 2006; Liekens et al., 2007; Bronckaers et al., 2009). TP in some cancer cells can also increase their invasive potential, although the exact mechanism remains unclear.
TP can also activate or inactivate several pyrimidines or pyrimidine nucleoside analogs with antiviral and antitumoral activity, such as inactivation of trifluorothymidine (TFT) (Heidelberger et al., 1964) and 5-fluoro-2'-deoxyruidine (van Laar et al., 1998), or activation of 5-fluorouracil (5-FU) (Schwartz et al., 1995) and 5-fluoro-5'-deoxyuridine (5'DFUR).
Homology The TYMP gene is conserved in chimpanzee, mouse, rat, and zebrafish.


Note Mutations in this gene have been associated with mitochondrial neurogastrointestinal encephalomyopathy (MNGIE). Multiple alternatively spliced variants, encoding the same protein, have been identified.

Implicated in

Entity Various cancer
Note TP in tumor sites can be expressed in the cancer cells, in the most malignant cells, tumor stromal cells (such as macrophages) or in the invasive part of the tumor (van Triest et al., 1999). A high TP expression and activity have been related to a poor outcome and increased angiogenesis. The TP gene is regulated by many other factors that are implicated in cancer, such as NFkB (de Bruin et al., 2004). TP regulates the expression of IL-8, and possibly also that of other genes, although the exact mechanism of this regulation is still unclear (Brown et al., 2000; Bijnsdorp et al., 2008). The high TP activity in the tumor can selectively activate the 5FU prodrug 5'-deoxy-5-fluorouridine to 5FU. 5'deoxy-5-fluorouridine is an intermediate of the oral 5FU prodrug Capecitabine (Xeloda) (de Bruin et al., 2006). On the other hand TP can inactivate the fluoropyrimidine trifluorothymidine (TFT), which is registered as the antiviral drug Viroptic® (De Clercq, 2004). An inhibitor of TP, TPI, will prevent inactivation of TFT. TAS-102 is a combination of TFT and TPI (in a molar ratio of 1:0.5) which is developed as an anticancer drug (Temmink et al., 2007).
Disease Gastrointestinal tumors (Fox et al., 1995; Yoshikawa et al., 1999; Kimura et al., 2002; Takebayashi et al., 1996), breast cancer (Moghaddam et al., 1995), bladder cancer (O'Brien et al., 1996).
Prognosis High expression is often related to a poor prognosis, an increased microvessel density and increased metastasis.
Abnormal Protein No fusion protein has been described.
Entity Rheumatoid arthritis
Note Elevated levels of (circulating) PD-ECGF (TP) were found in rheumatoid arthritis patients (Asai et al., 1993). In the sera and synovial fluids of patients suffering from rheumatoid arthritis PD-ECGF (TP) was detected at high levels (Asai et al., 1993). In addition, there was a significant positive correlation between PD-ECGF (TP) levels in synovial fluid and in serum (Asai et al., 1993). The elevated PD-ECGF (TP) levels presumably arise through induction of PD-ECGF (TP) in synoviocytes, resulting from aberrant production of cytokines like TNF-alpha and IL-1 (Waguri et al., 1997).
Entity Atherosclerosis
Note TP is expressed in atherosclerosis. Macrophages, foam cells and giant cells from both aortic and coronary plaques expressed TP, suggesting that TP may play a role in the pathogenesis of atherosclerosis (Boyle et al., 2000).
Entity Psoriasis
Note Increased PD-ECGF (TP) mRNA and immunoreactivity were found in lesional psoriasis compared to the non-lesional skin (Creamer et al., 1997). In another study it was reported that the thymidine phosphorylase activity was twenty-fold higher in psoriatic lesions than in normal skin (Hammerberg et al., 1991).
Entity Inflammatory bowel disease
Note In inflammatory bowel disease, TP has been found to be overexpressed, predominantly in macrophages and fibroblasts of the inflamed colonic mucosa. The grade of expression augmented with an increasing grade of inflammation. In addition, TP was found in the endothelial cells of the inflamed colonic mucosa (Giatromanolaki et al., 2003; Saito et al., 2003).
Entity Chronic glomerulonephritis
Note TP is upregulated in chronic glomerulonephritis (a renal disease characterized by inflammation of the glomeruli) where it probably plays a critical role in the progression of interstitial fibrosis (Wang et al., 2006).
Entity Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE)
Note An autosomal recessive disorder involving DNA alterations (Bardosi et al., 1987). Gene mutations in the TP gene include missense, splice sites microdeletions and single nucleotide insertions (Spinazzola et al., 2002; Nishino et al., 2000). These mutations are associated with a severe reduction in TP activity. This leads to increased thymidine plasma levels, and increased deoxyuridine levels (which is also a substrate for TP).
Prognosis Not determined.


High concentrations of immunoreactive gliostatin/platelet-derived endothelial cell growth factor in synovial fluid and serum of rheumatoid arthritis.
Asai K, Hirano T, Matsukawa K, Kusada J, Takeuchi M, Otsuka T, Matsui N, Kato T.
Clin Chim Acta. 1993 Sep 17;218(1):1-4.
PMID 7507805
Myo-, neuro-, gastrointestinal encephalopathy (MNGIE syndrome) due to partial deficiency of cytochrome-c-oxidase. A new mitochondrial multisystem disorder.
Bardosi A, Creutzfeldt W, DiMauro S, Felgenhauer K, Friede RL, Goebel HH, Kohlschutter A, Mayer G, Rahlf G, Servidei S, et al.
Acta Neuropathol. 1987;74(3):248-58.
PMID 2823522
Human platelet-derived endothelial cell growth factor is homologous to Escherichia coli thymidine phosphorylase.
Barton GJ, Ponting CP, Spraggon G, Finnis C, Sleep D.
Protein Sci. 1992 May;1(5):688-90.
PMID 1304367
The role of platelet-derived endothelial cell growth factor/thymidine phosphorylase in tumor behavior.
Bijnsdorp IV, de Bruin M, Laan AC, Fukushima M, Peters GJ.
Nucleosides Nucleotides Nucleic Acids. 2008 Jun;27(6):681-91. (REVIEW)
PMID 18600526
Expression of angiogenic factor thymidine phosphorylase and angiogenesis in human atherosclerosis.
Boyle JJ, Wilson B, Bicknell R, Harrower S, Weissberg PL, Fan TP.
J Pathol. 2000 Oct;192(2):234-42.
PMID 11004701
The dual role of thymidine phosphorylase in cancer development and chemotherapy.
Bronckaers A, Gago F, Balzarini J, Liekens S.
Med Res Rev. 2009 Nov;29(6):903-53. (REVIEW)
PMID 19434693
Thymidine phosphorylase induces carcinoma cell oxidative stress and promotes secretion of angiogenic factors.
Brown NS, Jones A, Fujiyama C, Harris AL, Bicknell R.
Cancer Res. 2000 Nov 15;60(22):6298-302.
PMID 11103787
Overexpression of the angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase in psoriatic epidermis.
Creamer D, Jaggar R, Allen M, Bicknell R, Barker J.
Br J Dermatol. 1997 Dec;137(6):851-5.
PMID 9470899
Antiviral drugs in current clinical use.
De Clercq E.
J Clin Virol. 2004 Jun;30(2):115-33.
PMID 15125867
Catabolism of thymidine in human blood platelets: purification and properties of thymidine phosphorylase.
Desgranges C, Razaka G, Rabaud M, Bricaud H.
Biochim Biophys Acta. 1981 Jul 27;654(2):211-8.
PMID 7284378
Cytokines induce thymidine phosphorylase expression in tumor cells and make them more susceptible to 5'-deoxy-5-fluorouridine.
Eda H, Fujimoto K, Watanabe S, Ura M, Hino A, Tanaka Y, Wada K, Ishitsuka H.
Cancer Chemother Pharmacol. 1993;32(5):333-8.
PMID 8339382
Platelet-derived endothelial cell growth factor/thymidine phosphorylase expression in normal tissues: an immunohistochemical study.
Fox SB, Moghaddam A, Westwood M, Turley H, Bicknell R, Gatter KC, Harris AL.
J Pathol. 1995 Jun;176(2):183-90.
PMID 7636628
Angiogenic factor.
Furukawa T, Yoshimura A, Sumizawa T, Haraguchi M, Akiyama S, Fukui K, Ishizawa M, Yamada Y.
Nature. 1992 Apr 23;356(6371):668.
PMID 1570012
Hypoxia inducible factor 1alpha and 2alpha overexpression in inflammatory bowel disease.
Giatromanolaki A, Sivridis E, Maltezos E, Papazoglou D, Simopoulos C, Gatter KC, Harris AL, Koukourakis MI.
J Clin Pathol. 2003 Mar;56(3):209-13.
PMID 12610101
Cancer Res. 1964 Dec;24:1979-85.
PMID 14247510
Organization and chromosomal localization of the human platelet-derived endothelial cell growth factor gene.
Hagiwara K, Stenman G, Honda H, Sahlin P, Andersson A, Miyazono K, Heldin CH, Ishikawa F, Takaku F.
Mol Cell Biol. 1991 Apr;11(4):2125-32.
PMID 2005900
Elevated thymidine phosphorylase activity in psoriatic lesions accounts for the apparent presence of an epidermal "growth inhibitor," but is not in itself growth inhibitory.
Hammerberg C, Fisher GJ, Voorhees JJ, Cooper KD.
J Invest Dermatol. 1991 Aug;97(2):286-90.
PMID 2071939
Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor.
Ishikawa F, Miyazono K, Hellman U, Drexler H, Wernstedt C, Hagiwara K, Usuki K, Takaku F, Risau W, Heldin CH.
Nature. 1989 Apr 13;338(6216):557-62.
PMID 2467210
Correlation between expression levels of thymidine phosphorylase (dThdPase) and clinical features in human gastric carcinoma.
Kimura H, Konishi K, Kaji M, Maeda K, Yabushita K, Miwa A.
Hepatogastroenterology. 2002 May-Jun;49(45):882-6.
PMID 12064013
Targeting platelet-derived endothelial cell growth factor/thymidine phosphorylase for cancer therapy.
Liekens S, Bronckaers A, Perez-Perez MJ, Balzarini J.
Biochem Pharmacol. 2007 Dec 3;74(11):1555-67. Epub 2007 May 16. (REVIEW)
PMID 17572389
Purification and properties of an endothelial cell growth factor from human platelets.
Miyazono K, Okabe T, Urabe A, Takaku F, Heldin CH.
J Biol Chem. 1987 Mar 25;262(9):4098-103.
PMID 3549724
Thymidine phosphorylase is angiogenic and promotes tumor growth.
Moghaddam A, Zhang HT, Fan TP, Hu DE, Lees VC, Turley H, Fox SB, Gatter KC, Harris AL, Bicknell R.
Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):998-1002.
PMID 7532308
Mitochondrial neurogastrointestinal encephalomyopathy: an autosomal recessive disorder due to thymidine phosphorylase mutations.
Nishino I, Spinazzola A, Papadimitriou A, Hammans S, Steiner I, Hahn CD, Connolly AM, Verloes A, Guimaraes J, Maillard I, Hamano H, Donati MA, Semrad CE, Russell JA, Andreu AL, Hadjigeorgiou GM, Vu TH, Tadesse S, Nygaard TG, Nonaka I, Hirano I, Bonilla E, Rowland LP, DiMauro S, Hirano M.
Ann Neurol. 2000 Jun;47(6):792-800.
PMID 10852545
Expression of the angiogenic factor thymidine phosphorylase/platelet-derived endothelial cell growth factor in primary bladder cancers.
O'Brien TS, Fox SB, Dickinson AJ, Turley H, Westwood M, Moghaddam A, Gatter KC, Bicknell R, Harris AL.
Cancer Res. 1996 Oct 15;56(20):4799-804.
PMID 8841001
Expression of platelet-derived endothelial cell growth factor in inflammatory bowel disease.
Saito S, Tsuno NH, Sunami E, Hori N, Kitayama J, Kazama S, Okaji Y, Kawai K, Kanazawa T, Watanabe T, Shibata Y, Nagawa H.
J Gastroenterol. 2003;38(3):229-37.
PMID 12673445
Thymidine phosphorylase mediates the sensitivity of human colon carcinoma cells to 5-fluorouracil.
Schwartz EL, Baptiste N, Wadler S, Makower D.
J Biol Chem. 1995 Aug 11;270(32):19073-7.
PMID 7642571
Thymidine phosphorylase from Escherichia coli.
Schwartz M.
Methods Enzymol. 1978;51:442-5.
PMID 357904
Altered thymidine metabolism due to defects of thymidine phosphorylase.
Spinazzola A, Marti R, Nishino I, Andreu AL, Naini A, Tadesse S, Pela I, Zammarchi E, Donati MA, Oliver JA, Hirano M.
J Biol Chem. 2002 Feb 8;277(6):4128-33. Epub 2001 Dec 3.
PMID 11733540
Regional localization of the human platelet-derived endothelial cell growth factor (ECGF1) gene to chromosome 22q13.
Stenman G, Sahlin P, Dumanski JP, Hagiwara K, Ishikawa F, Miyazono K, Collins VP, Heldin CH.
Cytogenet Cell Genet. 1992;59(1):22-3.
PMID 1733667
The activity and expression of thymidine phosphorylase in human solid tumours.
Takebayashi Y, Yamada K, Miyadera K, Sumizawa T, Furukawa T, Kinoshita F, Aoki D, Okumura H, Yamada Y, Akiyama S, Aikou T.
Eur J Cancer. 1996 Jun;32A(7):1227-32.
PMID 8758258
Aberrant production of gliostatin/platelet-derived endothelial cell growth factor in rheumatoid synovium.
Takeuchi M, Otsuka T, Matsui N, Asai K, Hirano T, Moriyama A, Isobe I, Eksioglu YZ, Matsukawa K, Kato T, et al.
Arthritis Rheum. 1994 May;37(5):662-72.
PMID 8185693
Therapeutic potential of the dual-targeted TAS-102 formulation in the treatment of gastrointestinal malignancies.
Temmink OH, Emura T, de Bruin M, Fukushima M, Peters GJ.
Cancer Sci. 2007 Jun;98(6):779-89. Epub 2007 Apr 18. (REVIEW)
PMID 17441963
Covalent linkage between nucleotides and platelet-derived endothelial cell growth factor.
Usuki K, Miyazono K, Heldin CH.
J Biol Chem. 1991 Oct 25;266(30):20525-31.
PMID 1939103
Gliostatin/platelet-derived endothelial cell growth factor as a clinical marker of rheumatoid arthritis and its regulation in fibroblast-like synoviocytes.
Waguri Y, Otsuka T, Sugimura I, Matsui N, Asai K, Moriyama A, Kato T.
Br J Rheumatol. 1997 Mar;36(3):315-21.
PMID 9133962
Upregulation of thymidine phosphorylase in chronic glomerulonephritis and its role in tubulointerstitial injury.
Wang EH, Goh YB, Moon IS, Park CH, Lee KH, Kang SH, Kang CS, Choi YJ.
Nephron Clin Pract. 2006;102(3-4):c133-42. Epub 2005 Nov 10.
PMID 16282698
Thymidine phosphorylase/platelet-derived endothelial cell growth factor is upregulated in advanced solid types of gastric cancer.
Yoshikawa T, Suzuki K, Kobayashi O, Sairenji M, Motohashi H, Tsuburaya A, Nakamura Y, Shimizu A, Yanoma S, Noguchi Y.
Br J Cancer. 1999 Mar;79(7-8):1145-50.
PMID 10098749
The Sp1 transcription factor contributes to the tumor necrosis factor-induced expression of the angiogenic factor thymidine phosphorylase in human colon carcinoma cells.
Zhu GH, Lenzi M, Schwartz EL.
Oncogene. 2002 Dec 5;21(55):8477-85.
PMID 12466967
Expression of the angiogenic factor thymidine phosphorylase in THP-1 monocytes: induction by autocrine tumor necrosis factor-alpha and inhibition by aspirin.
Zhu GH, Schwartz EL.
Mol Pharmacol. 2003 Nov;64(5):1251-8.
PMID 14573775
Role of platelet derived endothelial cell growth factor/ thymidine phosphorylase in health and disease.
de Bruin M, Temmink OH, Hoekman K, Pinedo H, Peters GJ.
Cancer Therapy. 2006;4:99-124. (REVIEW)
Comparison of 5-fluoro-2'-deoxyuridine with 5-fluorouracil and their role in the treatment of colorectal cancer.
van Laar JA, Rustum YM, Ackland SP, van Groeningen CJ, Peters GJ.
Eur J Cancer. 1998 Feb;34(3):296-306.
PMID 9640213
Prognostic role of thymidylate synthase, thymidine phosphorylase/platelet-derived endothelial cell growth factor, and proliferation markers in colorectal cancer.
van Triest B, Pinedo HM, Blaauwgeers JL, van Diest PJ, Schoenmakers PS, Voorn DA, Smid K, Hoekman K, Hoitsma HF, Peters GJ.
Clin Cancer Res. 2000 Mar;6(3):1063-72.
PMID 10741735


This paper should be referenced as such :
Bijnsdorp, IV ; Peters, GJ
TYMP (thymidine phosphorylase)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(12):1170-1174.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)TYMP   3148
LRG (Locus Reference Genomic)LRG_727
Atlas Explorer : (Salamanque)TYMP
Entrez_Gene (NCBI)TYMP    thymidine phosphorylase
GeneCards (Weizmann)TYMP
Ensembl hg19 (Hinxton)ENSG00000025708 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000025708 [Gene_View]  ENSG00000025708 [Sequence]  chr22:50525753-50530012 [Contig_View]  TYMP [Vega]
ICGC DataPortalENSG00000025708
Genatlas (Paris)TYMP
SOURCE (Princeton)TYMP
Genetics Home Reference (NIH)TYMP
Genomic and cartography
GoldenPath hg38 (UCSC)TYMP  -     chr22:50525753-50530012 -  22q13.33   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TYMP  -     22q13.33   [Description]    (hg19-Feb_2009)
GoldenPathTYMP - 22q13.33 [CytoView hg19]  TYMP - 22q13.33 [CytoView hg38]
Genome Data Viewer NCBITYMP [Mapview hg19]  
OMIM131222   603041   
Gene and transcription
Genbank (Entrez)AK057214 AK225269 AK298691 AK301194 AK314716
RefSeq transcript (Entrez)NM_001113755 NM_001113756 NM_001257988 NM_001257989 NM_001953
Consensus coding sequences : CCDS (NCBI)TYMP
Gene ExpressionTYMP [ NCBI-GEO ]   TYMP [ EBI - ARRAY_EXPRESS ]   TYMP [ SEEK ]   TYMP [ MEM ]
Gene Expression Viewer (FireBrowse)TYMP [ Firebrowse - Broad ]
GenevisibleExpression of TYMP in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1890
GTEX Portal (Tissue expression)TYMP
Human Protein AtlasENSG00000025708-TYMP [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP19971   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP19971  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP19971
Catalytic activity : Enzyme2.4.2.4 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)THYMID_PHOSPHORYLASE (PS00647)   
Domains : Interpro (EBI)Glycosyl_Trfase_fam3    Glycosyl_Trfase_fam3_N_dom    Glycosyl_Trfase_fam3_N_dom)sf    Nuc_phospho_transferase    PYNP-like_C_sf    PYNP_C    Pyrmidine_PPas_bac/euk    Pyrmidine_PPase_CS    Thymidine/pyrmidine_PPase   
Domain families : Pfam (Sanger)Glycos_trans_3N (PF02885)    Glycos_transf_3 (PF00591)    PYNP_C (PF07831)   
Domain families : Pfam (NCBI)pfam02885    pfam00591    pfam07831   
Domain families : Smart (EMBL)PYNP_C (SM00941)  
Conserved Domain (NCBI)TYMP
PDB (RSDB)1UOU    2J0F    2WK5    2WK6   
PDB Europe1UOU    2J0F    2WK5    2WK6   
PDB (PDBSum)1UOU    2J0F    2WK5    2WK6   
PDB (IMB)1UOU    2J0F    2WK5    2WK6   
Structural Biology KnowledgeBase1UOU    2J0F    2WK5    2WK6   
SCOP (Structural Classification of Proteins)1UOU    2J0F    2WK5    2WK6   
CATH (Classification of proteins structures)1UOU    2J0F    2WK5    2WK6   
AlphaFold pdb e-kbP19971   
Human Protein Atlas [tissue]ENSG00000025708-TYMP [tissue]
Protein Interaction databases
IntAct (EBI)P19971
Ontologies - Pathways
Ontology : AmiGOmitochondrial genome maintenance  angiogenesis  1,4-alpha-oligoglucan phosphorylase activity  protein binding  cytosol  cytosol  pyrimidine nucleobase metabolic process  pyrimidine nucleoside metabolic process  pyrimidine nucleoside metabolic process  chemotaxis  signal transduction  growth factor activity  thymidine phosphorylase activity  thymidine phosphorylase activity  pyrimidine-nucleoside phosphorylase activity  cell differentiation  regulation of myelination  protein homodimerization activity  pyrimidine nucleoside salvage  dTMP catabolic process  pyrimidine nucleoside catabolic process  regulation of transmission of nerve impulse  regulation of gastric motility  
Ontology : EGO-EBImitochondrial genome maintenance  angiogenesis  1,4-alpha-oligoglucan phosphorylase activity  protein binding  cytosol  cytosol  pyrimidine nucleobase metabolic process  pyrimidine nucleoside metabolic process  pyrimidine nucleoside metabolic process  chemotaxis  signal transduction  growth factor activity  thymidine phosphorylase activity  thymidine phosphorylase activity  pyrimidine-nucleoside phosphorylase activity  cell differentiation  regulation of myelination  protein homodimerization activity  pyrimidine nucleoside salvage  dTMP catabolic process  pyrimidine nucleoside catabolic process  regulation of transmission of nerve impulse  regulation of gastric motility  
Pathways : KEGGPyrimidine metabolism    Drug metabolism - other enzymes    Bladder cancer   
REACTOMEP19971 [protein]
REACTOME PathwaysR-HSA-73621 [pathway]   
NDEx NetworkTYMP
Atlas of Cancer Signalling NetworkTYMP
Wikipedia pathwaysTYMP
Orthology - Evolution
GeneTree (enSembl)ENSG00000025708
Phylogenetic Trees/Animal Genes : TreeFamTYMP
Homologs : HomoloGeneTYMP
Homology/Alignments : Family Browser (UCSC)TYMP
Gene fusions - Rearrangements
Fusion : MitelmanTYMP::PPP6R2 [22q13.33/22q13.33]  
Fusion : FusionGDB2.4.2.4   
Fusion : QuiverTYMP
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTYMP [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TYMP
Exome Variant ServerTYMP
GNOMAD BrowserENSG00000025708
Varsome BrowserTYMP
ACMGTYMP variants
Genomic Variants (DGV)TYMP [DGVbeta]
DECIPHERTYMP [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTYMP 
ICGC Data PortalTYMP 
TCGA Data PortalTYMP 
Broad Tumor PortalTYMP
OASIS PortalTYMP [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTYMP  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DTYMP
Mutations and Diseases : HGMDTYMP
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)TYMP
DoCM (Curated mutations)TYMP
CIViC (Clinical Interpretations of Variants in Cancer)TYMP
NCG (London)TYMP
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM131222    603041   
Genetic Testing Registry TYMP
NextProtP19971 [Medical]
Target ValidationTYMP
Huge Navigator TYMP [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDTYMP
Pharm GKB GenePA162407502
Pharm GKB PathwaysPA150653776   
Clinical trialTYMP
DataMed IndexTYMP
PubMed176 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
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