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TAB3  -  TGF-beta activated kinase 1/MAP3K7 binding...

Homo sapiens

Synonyms: MAP3K7IP3, Mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NAP1, NF-kappa-B-activating protein 1, TAB-3, ...
 
 
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Disease relevance of MAP3K7IP3

  • Essentially pure preparations of normal density eosinophils obtained from patients with hypereosinophilic syndrome (HES) were stimulated with complement factor 5a (C5a), platelet-activating factor (PAF), FMLP and neutrophil-activating peptide (NAP-1/IL-8) [1].
 

High impact information on MAP3K7IP3

 

Biological context of MAP3K7IP3

  • Here we present evidence that TAB2 and TAB3 are receptors that bind preferentially to lysine 63-linked polyubiquitin chains through a highly conserved zinc finger (ZnF) domain [2].
  • Based on these studies, we propose a role for post-transcriptional control of gene expression during neural induction in vertebrates and present a model whereby sustained BMP inhibition is promoted partly through the regulation of TGFbeta activated kinase (TAK1) activity by a novel TAK1-binding protein (TAB3) [5].
  • The centrosomal protein C-Nap1 is thought to play an important role in centrosome cohesion during interphase of the cell cycle [6].
 

Anatomical context of MAP3K7IP3

  • NAP-1 in fluid of unstimulated macrophages was 40 +/- 15 ng/ml [7].
  • The HPLC-CM elution profile of macrophage NAP-1 was identical to that of monocyte NAP-1, and the N-terminal sequence of the protein in one of the isolated peaks corresponded to that of monocyte-derived NAP-1 beta [7].
 

Associations of MAP3K7IP3 with chemical compounds

  • Our results indicate that TAB3 is phosphorylated via the SAPK2a/p38alpha pathway, whereas TAB2 is phosphorylated at two or more sites by both an SAPK2a/p38alpha-dependent and an SB 203580-independent kinase [8].
  • Therefore, LPS and zymosan particles were potent stimuli of the sequential release of LTB4 and NAP-1 from AM [3].
  • We determined if one of these attractants is neutrophil attractant/activating protein (NAP-1), which is secreted by blood monocytes stimulated by lipopolysaccharide (LPS) [7].
 

Analytical, diagnostic and therapeutic context of MAP3K7IP3

  • Culture fluids collected at 24 h were assayed for both neutrophil chemotactic activity and the concentration of NAP-1 as determined by a sandwich ELISA [7].

References

  1. Shape changes, exocytosis, and cytosolic free calcium changes in stimulated human eosinophils. Kernen, P., Wymann, M.P., von Tscharner, V., Deranleau, D.A., Tai, P.C., Spry, C.J., Dahinden, C.A., Baggiolini, M. J. Clin. Invest. (1991) [Pubmed]
  2. TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Kanayama, A., Seth, R.B., Sun, L., Ea, C.K., Hong, M., Shaito, A., Chiu, Y.H., Deng, L., Chen, Z.J. Mol. Cell (2004) [Pubmed]
  3. Macrophages cultured in vitro release leukotriene B4 and neutrophil attractant/activation protein (interleukin 8) sequentially in response to stimulation with lipopolysaccharide and zymosan. Rankin, J.A., Sylvester, I., Smith, S., Yoshimura, T., Leonard, E.J. J. Clin. Invest. (1990) [Pubmed]
  4. Identification of a human NF-kappaB-activating protein, TAB3. Jin, G., Klika, A., Callahan, M., Faga, B., Danzig, J., Jiang, Z., Li, X., Stark, G.R., Harrington, J., Sherf, B. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. Gene profiling during neural induction in Xenopus laevis: regulation of BMP signaling by post-transcriptional mechanisms and TAB3, a novel TAK1-binding protein. Muñoz-Sanjuán, I., Bell, E., Altmann, C.R., Vonica, A., Brivanlou, A.H. Development (2002) [Pubmed]
  6. The mechanism regulating the dissociation of the centrosomal protein C-Nap1 from mitotic spindle poles. Mayor, T., Hacker, U., Stierhof, Y.D., Nigg, E.A. J. Cell. Sci. (2002) [Pubmed]
  7. Secretion of neutrophil attractant/activation protein by lipopolysaccharide-stimulated lung macrophages determined by both enzyme-linked immunosorbent assay and N-terminal sequence analysis. Sylvester, I., Rankin, J.A., Yoshimura, T., Tanaka, S., Leonard, E.J. Am. Rev. Respir. Dis. (1990) [Pubmed]
  8. TAB3, a new binding partner of the protein kinase TAK1. Cheung, P.C., Nebreda, A.R., Cohen, P. Biochem. J. (2004) [Pubmed]
 
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