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Dual specificity phosphatase 13

TMDP, MDSP, muscle-restricted dual specificity phosphatase, DUSP13, LMW-DSP6
Members of the protein-tyrosine phosphatase superfamily cooperate with protein kinases to regulate cell proliferation and differentiation. This superfamily is separated into two families based on the substrate that is dephosphorylated. One family, the dual specificity phosphatases (DSPs) acts on both phosphotyrosine and phosphoserine/threonine residues. This gene encodes different but related DSP proteins through the use of non-overlapping open reading frames, alternate splicing, and presumed different transcription promoters. Expression of the distinct proteins from this gene has been found to be tissue specific and the proteins may be involved in postnatal development of specific tissues. A protein encoded by the upstream ORF was found in skeletal muscle, whereas the encoded protein from the downstream ORF was found only in testis. In mouse, a similar pattern of expression was found. Multiple alternatively spliced transcript variants were described, but the full-length sequence of only some were determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DSP, VHR, ACID, JNK, fibrillin-1
Papers on TMDP
Methylation of leukocyte DNA and ovarian cancer: relationships with disease status and outcome.
Goode et al., Kansas City, United States. In Bmc Med Genomics, 2013
The top association was observed for the methylation probe cg04834572 located approximately 315 kb upstream of DUSP13 (p = 1.6 x10-14).
DUSP13B/TMDP inhibits stress-activated MAPKs and suppresses AP-1-dependent gene expression.
Shima et al., Japan. In Mol Cell Biochem, 2011
data suggest an important role for DUSP13B in protection from external stress during spermatogenesis
Identification and characterization of DUSP27, a novel dual-specific protein phosphatase.
Mustelin et al., Los Angeles, United States. In Febs Lett, 2007
DUSP27 is structurally similar to other small DSPs, like VHR and DUSP13.
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity.
Kim et al., Taejŏn, South Korea. In Proteins, 2007
Here, we report the crystal structure of human TMDP at a resolution of 2.4 A. In spite of high sequence similarity with other DSPs, the crystal structure of TMDP shows distinct structural motifs and surface propertie
Characterization of two distinct dual specificity phosphatases encoded in alternative open reading frames of a single gene located on human chromosome 10q22.2.
Tonks et al., New York City, United States. In J Biol Chem, 2004
expression of both MDSP and TMDP proteins was markedly increased at the 3rd week after birth and continued to increase gradually into adulthood, implying that the physiological functions of both DSPs are specific to the mature/late-developing organs
A novel low-molecular-mass dual-specificity phosphatase, LDP-2, with a naturally occurring substitution that affects substrate specificity.
Kikuchi et al., Sapporo, Japan. In J Biochem, 2002
We have identified a novel dual-specificity phosphatase (DSP), called LDP-2 (low-molecular-mass DSP-2), composed of 220 amino acid residues showing high sequence homology to VHR and LDP-1/TMDP, which belong to a family of DSPs with low molecular masses.
A growing family of dual specificity phosphatases with low molecular masses.
Matsuda et al., Nagoya, Japan. In J Biochem, 2001
LMW-DSP6 was found to be identical to recently cloned TMDP, and LMW-DSP11 seemed to be a mouse ortholog of human VHR.
Molecular cloning and characterization of a novel dual-specificity protein phosphatase possibly involved in spermatogenesis.
Kikuchi et al., Sapporo, Japan. In Biochem J, 2000
In the present study, we identified a novel DSP, termed TMDP (testis- and skeletal-muscle-specific DSP).
The effect of Syntex adjuvant formulation (SAF-m) on humoral immunity to the influenza virus in the mouse.
Levner et al., United States. In Vaccine, 1997
The threonyl-MDP (t-MDP) component of the adjuvant played no role in this activity.
Origin of the ATP formed during the light-dependent oxygen uptake catalyzed by Rhodospirillum rubrum chromatophores.
Ramírez et al., In Z Naturforsch C, 1975
The oxygen uptake which is observed when Rhodospirillum rubrum chromatophores are illuminated under air and in the presence of reduced 2, 6-dichlorophenolindophenol (DCIP), 2, 3, 5, 6-tetra-methyl-P-phenylenediamine (diaminodurene, DAD) or N, N'-tetramethyl-p-phenylenediamine (TMDP) depends on the electron-donor concentration according to the equation of Michaelis-Menten.
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