Vaccinia H1-related phosphatase (VHR) is classified as a dual-specificity phosphatase (DUSP); and the other name is dual-specificity phosphatase 3 (DUSP3). DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. Unlike typical DUSPs; VHR lacks mitogen-activated protein kinase (MAPK)-binding domain; and shows poor activity against MAPKs. VHR often act on bisphosphorylated protein substrates; it displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. VHR has been identified as a novel regulator of extracellular regulated kinases (ERKs). VHR is responsible for the rapid inactivation of ERK following stimulation and for its repression in quiescent cells. VHR is a negative regulator of the Erk and Jnk pathways in T cells and; therefore; may play a role in aspects of T lymphocyte physiology that depend on these kinases.
Human DUSP3 belongs to the dual specificity protein phosphatase subfamily. DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSPs are major modulators of critical signalling pathways that are dysregulated in various diseases. They negatively regulate members of the mitogen-activated protein kinase superfamily; which are associated with cellular proliferation and differentiation. DUSP3 is expressed in human tissues including breast and ovarian.DUSP3 shows activity both for tyrosine-protein phosphate and serine-protein phosphate; but displays a strong preference toward phosphotyrosines. Human DUSP3 specifically dephosphorylates and inactivates ERK1 and ERK2.
Deoxyuridine 5'-Triphosphate Nucleotidohydrolase Mitochondrial (dUTPase) belongs to the dUTPase family. dUTPase exits as a homotrimer and is involved in nucleotide metabolism. dUTPase produces dUMP; the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. The dUTPase increase in PCR product yield; length and fidelity enables further down-stream applications. These effects make dUTPase useful in PCR fidelity and yield-sensitive applications. dUTPase is specific for dUTP and is critical for the fidelity of DNA replication and repair.
Human Dynein Cytoplasmic Light Chain 1 (DYNLL1) has been identified as a protein that interacts with NOS1, leading to NOS1 inhibition. NOS1 dimer is destabilized after binding DYNLL1 a conformation necessary activity, and it regulate numerous biologic processes throughits effects on nitric oxide synthase activity. DYNLL1 is widely expressed, with higher expression in testis and moderate expression in brain.
Dual specificity tyrosine-phosphorylation-regulated kinase 3, also known as Regulatory erythroid kinase, REDK and DYRK3, is a nucleus protein which belongs to theprotein kinase superfamily, CMGC Ser/Thr protein kinase family and MNB/DYRK subfamily. DYRKs are an emerging family of dual-specificity kinases that play key roles in cell proliferation, survival, and development. DYRK3 contains oneprotein kinase domain. Isoform 1 and isoform 2 of DYRK3 are highly expressed in testis and in hematopoietic tissue such as fetal liver, and bone marrow. Isoform 2 of DYRK3 is the predominant form in testis. Isoform 1 of DYRK3 is the predominant form in fetal liver and bone marrow. Isoform 1 and isoform 2 are present at low levels in heart, pancreas, lymph node, and thymus. DYRK3 is a negative regulator of EPO-dependent erythropoiesis. It may place an upper limit on red cell production during stress erythropoiesis. DYRK3 inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. It may also act by regulating CREB/CRE signaling. DYRK3 proved to effectively inhibit NFAT (nuclear factor of activated T cells) transcriptional response pathways and to co-immunoprecipitate with NFATc3. DYRK3 attenuates (and possibly apportions) red cell production selectively during anemia.
E2F-2 (viral E2-associated factor 2) is a 50 55 kDa member of the E2F/DP family of transcription factors. It is principally expressed by placenta, and forms a DNA activating E2F heterodimeric complex with DP-1 or-2. This complex, when active, promotes cell cycle progression. In quiescent cells, association with the retinoblastoma-tumor suppressor gene product termed pRB suppresses its activity. Human E2F 2 is 437 amino acids (aa) in length and contains a CDK2 binding region (aa 65 105), a DNA binding domain (aa 107 196), a dimerization segment (aa 197 289), a transactivation region (aa 359 437), and a pRB binding domain (aa 410 427). There are two potential alternate start sites at Met197 and Met342, and one splice variant that shows a two aa substitution for aa 349 437. Over aa 308 437, human E2F-2 is 72% aa identical to mouse E2F-2.
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