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0TYPH_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionThymidine phosphorylase precursor (ec (tdrpase) (tp) (platelet-derived endothelial cell growth factor) (pd-ecgf) (gliostatin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005161 platelet-derived growth factor receptor bin... (TAS)
0009032 thymidine phosphorylase activity (TAS)
0006260 DNA replication (TAS)
0000002 mitochondrial genome maintenance (TAS)
0006220 pyrimidine nucleotide metabolism (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
The glycosyl transferase family includes anthranilate phosphoribosyltransferase (TrpD. and thymidine phosphorylase (). All these proteins can transfer a phosphorylated ribose substrate. Thymidine phosphorylase () catalyses the reversible phosphorolysis of thymidine.eoxyuridine and their analogues to their respective bases and 2-deoxyribose 1-phosphate. This enzyme regulates the availability of thymidine and is therefore essential to nucleic acid metabolism.
  IPR000312:Glycosyl transferase, family 3
This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases . It has slightly different conformations in different members of this family. For example.n pyrimidine nucleoside phosphorylase (PYNP. there is an added three-stranded anti-parallel beta sheet as compared to other members of the family.uch as E. coli thymidine phosphorylase (TP. . The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer .
  IPR013102:Pyrimidine nucleoside phosphorylase, C-terminal
Two highly similar activities are represented in this group: thymidine phosphorylase (TP.ene deoA. and pyrimidine-nucleoside phosphorylase (PyNP.ene pdp.. Both are dimeric enzymes that function in the salvage pathway to catalyse the reversible phosphorolysis of pyrimidine nucleosides to the free base and sugar moieties. In the case of thymidine phosphorylase.hymidine (and to a lesser extent.-deoxyuridine) is lysed to produce thymine (or uracil) and 2-deoxyribose-1-phosphate. Pyrimidine-nucleoside phosphorylase performs the analogous reaction on thymidine (to produce the same products) and uridine (to produce uracil and ribose-1-phosphate). PyNP is typically the only pyrimidine nucleoside phosphorylase encoded by Gram positive bacteria.hile eukaryotes and proteobacteria encode two: TP.nd the unrelated uridine phosphorylase. In humans.P was originally characterized as platelet-derived endothelial cell growth factor and gliostatin . Structurally.he enzymes are homodimers.ach composed of a rigid all alpha-helix lobe and a mixed alpha-helix/beta-sheet lobe.hich are connected by a flexible hinge . Prior to substrate binding.he lobes are separated by a large cleft. A functional active site and subsequent catalysis occurs upon closing of the cleft. The active site.omposed of a phosphate binding site and a (deoxy)ribonucleotide binding site within the cleft region.s highly conserved between the two enzymes of this group. Active site residues (Escherichia coli DeoA numbering) include the phosphate binding Lys84 and Ser86 (close to a glycine-rich loop).er113.nd Thr123.nd the pyrimidine nucleoside-binding Arg171.er186.nd Lys190. Sequence comparison between the active site residues for both enzymes reveals only one difference .hich has been proposed to partially mediate substrate specificity. In TP.osition 111 is a methionine.hile the analogous position in PyNP is lysine. It should be noted that the uncharacterised archaeal members of this family differ in a number of respects from either of the characterized activities. The residue at position 108 is lysine.ndicating the activity might be PyNP-like (though the determinants of substrate specificity have not been fully elucidated). Position 171 is glutamate (negative charge side chain) rather than arginine (positive charge side chain). In addition. large loop that may "lock in" the substrates within the active site is much smaller than in the characterized members. It is not clear what effect these and other differences have on activity and specificity.
  IPR000053:Pyrimidine-nucleoside phosphorylase
SequencesProtein: TYPH_HUMAN (482 aa)
mRNA: NM_001953
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00758
  Level 3 annotation:
    thymidine phosphorylase
  Level 2 annotation:
    Purine metabolism
    Pyrimidine metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 55 residues, 49311049-49311213Exon2: 49 residues, 49311295-49311436Exon3: 79 residues, 49311540-49311771Exon4: 56 residues, 49311870-49312033Exon5: 41 residues, 49312459-49312578Exon6: 45 residues, 49312882-49313012Exon7: 35 residues, 49313806-49313905Exon8: 69 residues, 49314430-49314633Exon9: 76 residues, 49314790-49315014Exon10: 43 residues, 49315198-49315321Exon11: 2 residues, -Jump to TYPH_HUMAN  
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Loci Cluster (Details)Loci: 4580 49033457-49042216 ~-9K 25027(MAPK12)(-)Loci: 4581 49044269-49050906 ~-7K 25029(MAPK11)(-)Loci: 4582 49308864-49310838 ~-2K 25050(SCO2)(-)Loci: 4583 49311049-49315321 ~-4K 25051(ECGF1)(-)Loci: 4584 49354156-49363744 ~-10K 25054(CPT1B)(-)Loci: 4579 48998244-49025527 ~-27K 25025(TUBGCP6)(-)Link out to UCSC