Disease relevance of DUSP13

• In TMDP, the alpha1-beta1 loop, a substrate recognition motif is located further away from the active site loop in comparison to prototype DSP Vaccinia H1 related phophatase (VHR), which preferentially dephosphorylates tyrosine phosphorylated substrates and down-regulates MAP kinase signaling [1].

High impact information on DUSP13

• TMDP is not detectable in testis lysate in the first 3 weeks of life [2].
• We have identified a gene located on human chromosome 10q22.2, which utilizes alternative open reading frames (ORFs) to encode the following two distinct DSPs: the previously described testis and skeletal muscle-specific dual specificity phosphatase (TMDP) and a novel DSP, muscle-restricted dual specificity phosphatase (MDSP) [2].
• MDSP is expressed at very low levels in myotubes and early postnatal muscle [2].
• These data demonstrate that TMDP is a novel DSP abundantly expressed in the testis and suggest that TMDP may be involved in the regulation of meiosis and/or differentiation of testicular germ cells during spermatogenesis [3].
• An efficient four-component system consisting of acetamido-TEMPO/Cu(ClO4)2/TMDP/DABCO in DMSO has been developed for room-temperature aerobic alcohol oxidation [4].

Biological context of DUSP13

• Residues in the active site residues of TMDP are smaller in size and more hydrophobic than those of VHR [1].
• Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity [1].

Associations of DUSP13 with chemical compounds

• Three new hybrid inorganic-organic salts containing novel mixed haloanions of bismuth were synthesized by the solvothermal reaction of bismuth iodide with a haloacid, HX (X = Cl or Br), and the alkylamine 4,4'-trimethylenedipiperidine (TMDP) [5].
• TMDP has similar activities toward both tyrosine and threonine phosphorylated substrates, and is supposed to be involved in spermatogenesis [1].
• These differences in the active site of TMDP result in a flat and wide pocket structure, allowing equal binding of phosphotyrosine and phosphothreonine substrates [1].

Analytical, diagnostic and therapeutic context of DUSP13

• Northern-blot analysis revealed that TMDP is most abundantly expressed in the testis [3].

References