TYMP (gene)

TYMP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTYMP, thymidine phosphorylase, ECGF, ECGF1, MEDPS1, MNGIE, MTDPS1, PDECGF, TP, hPD-ECGF
External IDsOMIM: 131222; MGI: 1920212; HomoloGene: 1474; GeneCards: TYMP; OMA:TYMP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001953
NM_001113755
NM_001113756
NM_001257988
NM_001257989

NM_138302
NM_028405

RefSeq (protein)

NP_001107227
NP_001107228
NP_001244917
NP_001244918
NP_001944

NP_612175

Location (UCSC)Chr 22: 50.53 – 50.53 MbChr 15: 89.26 – 89.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

TYMP is a gene that encodes for the enzyme thymidine phosphorylase.[5][6] The TYMP gene is also known as ECGF1 (endothelial cell growth factor 1, platelet-derived) and MNGIE due to its role in MNGIE syndrome. [7]

Structure

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The TYMP gene is located on chromosome 22 in humans and contains 10 exons spanning more than 4.3 kb.

Function

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TYMP encodes for the enzyme thymidine phosphorylase. TYMP and thymidine phosphorylase are associated with angiogenesis, growth of endothelial cells, and mitochondrial neurogastrointestinal encephalomyopathy (MNGIE).

Thymidine phosphorylase is angiogenic growth factor which promotes angiogenesis in vivo and stimulates the in vitro growth of a variety of endothelial cells. Thymidine phosphorylase has a highly restricted target cell specificity acting only on endothelial cells, hence its alternative name of ECGF1. Because it limits glial cell proliferation, thymidine phosphorylase is also known as gliostatin. Thymidine phosphorylase activity in leukocytes from mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) patients was less than 5 percent of controls, indicating that loss-of-function mutations in TYMP cause MNGIE.[8]

Interactive pathway map

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Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

[[File:
FluoropyrimidineActivity_WP1601go to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to PubChem Compoundgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
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FluoropyrimidineActivity_WP1601go to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to PubChem Compoundgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
|alt=Fluorouracil (5-FU) Activity edit]]
Fluorouracil (5-FU) Activity edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000025708Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022615Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH (Jun 1992). "Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity". Biochem Biophys Res Commun. 184 (3): 1311–6. doi:10.1016/S0006-291X(05)80025-7. PMID 1590793.
  6. ^ Spinazzola A, Marti R, Nishino I, Andreu AL, Naini A, Tadesse S, Pela I, Zammarchi E, Donati MA, Oliver JA, Hirano M (Feb 2002). "Altered thymidine metabolism due to defects of thymidine phosphorylase". J Biol Chem. 277 (6): 4128–33. doi:10.1074/jbc.M111028200. PMID 11733540.
  7. ^ "Gene symbol report | HUGO Gene Nomenclature Committee".
  8. ^ "Entrez Gene: ECGF1 endothelial cell growth factor 1 (platelet-derived)".

Further reading

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