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Gene Review

MYCBP  -  MYC binding protein

Homo sapiens

Synonyms: AMY-1, AMY1, Associate of Myc 1, C-Myc-binding protein
 
 
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Disease relevance of MYCBP

 

High impact information on MYCBP

  • These results suggest that both AAT-1 and AMY-1 play roles in spermatogenesis [3].
  • AAT-1alpha was found to bind to and be colocalized in mitochondria with AMY-1 in human HeLa and mouse GC-1 cells [3].
  • AAT-1 was found to be specifically expressed in the testis during the course of spermatogenesis and also to be present in the spermatid and mature sperm, as was AMY-1 [3].
  • It was also found that the formation of the complex of AMY-1 with AKAP84/95 and RII prevented a catalytic subunit from binding to this AKAP complex, leading to suppression of PKA activity [4].
  • We have reported that a novel c-Myc-binding protein, AMY-1 (associate of Myc-1), stimulated the transcription activity of c-Myc [5].
 

Biological context of MYCBP

  • AMY-1, which mostly localizes in the cytoplasm, translocates into the nucleus in the S phase of the cell cycle upon an increase of c-myc expression, and may thus control the transcriptional activity of C-MYC [6].
  • AMY-1 was bound via its C-terminal region to the N-terminal region of C-MYC (amino acids nos 58-148) corresponding to the transactivation domain [6].
  • AMY-1 by itself did not recognize the E-box element, the MYC/Max binding sequence, nor did it transactivate via the element, but stimulated the activation of E-box-regulated transcription by MYC/Max [6].
  • We have isolated the cDNA encoding a novel c-Myc-binding protein, MM-1, by the yeast two-hybrid screening of a human HeLa cell cDNA library [7].
  • AMY-1 works as an inducer of human K562 cell differentiation upon induction of AraC [8].
 

Anatomical context of MYCBP

  • AMAP-1 was found to be specifically expressed in the testis and expressed post-meiotically in the testis, as was AMY-1 [9].
  • AMY-1 was found to bind to and be colocalized with AMAP-1 in human 293T and HeLa cells [9].
  • We show here that, using anti-AMY-1 antibodies we raised, AMY-1 localizes to the trans-Golgi network (TGN) and the nucleus [10].
  • The results showed that Sp1 was essential for AMY-1 expression in both cell lines and that GATA-1 is also necessary in K562 cells [8].
  • AMY-1 is a trigger for the erythrocyte differentiation of K562 cells [11].
 

Associations of MYCBP with chemical compounds

 

Physical interactions of MYCBP

  • All of the isoforms of AAT-1 were found to bind to and colocalized with AMY-1 in human cells [13].
 

Regulatory relationships of MYCBP

 

Other interactions of MYCBP

 

Analytical, diagnostic and therapeutic context of MYCBP

  • To explore the possible function of AMY-1, we have undertaken a search for interacting partners by co-immunoprecipitation experiments using cells stably expressing FLAG-tagged AMY-1 [10].
  • The isl-1 homeodomain binds to the AT-rich AMY element (-156 to -137) in the human amylin (hAMY) gene promoter, and electrophoretic mobility shift assay experiments using isl-1 specific antiserum detected the formation of an hAMY-isl-1 complex using nuclear extract from InR1 -G9 islet cells [15].
  • An alternative method for AMY1 typing by means of isoelectric focusing is proposed which allows the use of long-term stored saliva samples [16].

References

  1. MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer. Fujioka, Y., Taira, T., Maeda, Y., Tanaka, S., Nishihara, H., Iguchi-Ariga, S.M., Nagashima, K., Ariga, H. J. Biol. Chem. (2001) [Pubmed]
  2. Differential gene expression in neoplastic and human papillomavirus-immortalized oral keratinocytes. Rey, O., Baluda, M.A., Park, N.H. Oncogene (1999) [Pubmed]
  3. AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase. Yukitake, H., Furusawa, M., Taira, T., Iguchi-Ariga, S.M., Ariga, H. J. Biol. Chem. (2002) [Pubmed]
  4. AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex. Furusawa, M., Taira, T., Iguchi-Ariga, S.M., Ariga, H. J. Biol. Chem. (2002) [Pubmed]
  5. AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase. Furusawa, M., Ohnishi, T., Taira, T., Iguchi-Ariga, S.M., Ariga, H. J. Biol. Chem. (2001) [Pubmed]
  6. AMY-1, a novel C-MYC binding protein that stimulates transcription activity of C-MYC. Taira, T., Maëda, J., Onishi, T., Kitaura, H., Yoshida, S., Kato, H., Ikeda, M., Tamai, K., Iguchi-Ariga, S.M., Ariga, H. Genes Cells (1998) [Pubmed]
  7. MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc. Mori, K., Maeda, Y., Kitaura, H., Taira, T., Iguchi-Ariga, S.M., Ariga, H. J. Biol. Chem. (1998) [Pubmed]
  8. Molecular cloning of the mouse AMY-1 gene and identification of the synergistic activation of the AMY-1 promoter by GATA-1 and Sp1. Furusawa, M., Taira, T., Iguchi-Ariga, S.M., Ariga, H. Genomics (2003) [Pubmed]
  9. AMAP-1, a novel testis-specific AMY-1-binding protein, is differentially expressed during the course of spermatogenesis. Yukitake, H., Furusawa, M., Taira, T., Iguchi-Ariga, S.M., Ariga, H. Biochim. Biophys. Acta (2002) [Pubmed]
  10. AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors. Ishizaki, R., Shin, H.W., Iguchi-Ariga, S.M., Ariga, H., Nakayama, K. Genes Cells (2006) [Pubmed]
  11. AMY-1 is a trigger for the erythrocyte differentiation of K562 cells. Furusawa, M., Onishi, T., Taira, T., Iguchi-Ariga, S.M., Ariga, H. Int. J. Oncol. (2000) [Pubmed]
  12. Involvement of NF-kappaB and c-myc signaling pathways in the apoptosis of HL-60 cells induced by alkaloids of Tripterygium hypoglaucum (levl.) Hutch. Zhuang, W.J., Fong, C.C., Cao, J., Ao, L., Leung, C.H., Cheung, H.Y., Xiao, P.G., Fong, W.F., Yang, M.S. Phytomedicine (2004) [Pubmed]
  13. Structure and characterization of AAT-1 isoforms. Matsuda, E., Ishizaki, R., Taira, T., Iguchi-Ariga, S.M., Ariga, H. Biol. Pharm. Bull. (2005) [Pubmed]
  14. Identification of MYCBP as a beta-catenin/LEF-1 target using DNA microarray analysis. Jung, H.C., Kim, K. Life Sci. (2005) [Pubmed]
  15. Activation of amylin gene transcription by LIM domain homeobox gene isl-1. Wang, M., Drucker, D.J. Mol. Endocrinol. (1996) [Pubmed]
  16. Salivary enzyme polymorphisms (Set, Sgd and AMY1) in the Galician population. Boán, F., Caeiro, J.L. Hum. Hered. (1988) [Pubmed]
 
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