MYBL2

From Wikipedia, the free encyclopedia


V-myb myeloblastosis viral oncogene homolog (avian)-like 2
PDB rendering based on 1a5j.
Available structures: 1a5j, 2d9a
Identifiers
Symbol(s) MYBL2; B-MYB; BMYB; MGC15600
External IDs OMIM: 601415 MGI101785 HomoloGene1847
Orthologs
Human Mouse
Entrez 4605 17865
Ensembl ENSG00000101057 ENSMUSG00000017861
Uniprot P10244 P48972
Refseq NM_002466 (mRNA)
NP_002457 (protein)
NM_008652 (mRNA)
NP_032678 (protein)
Location Chr 20: 41.73 - 41.78 Mb Chr 2: 162.75 - 162.78 Mb
Pubmed search [1] [2]

V-myb myeloblastosis viral oncogene homolog (avian)-like 2, also known as MYBL2, is a human gene.

The protein encoded by this gene, a member of the MYB family of transcription factor genes, is a nuclear protein involved in cell cycle progression. The encoded protein is phosphorylated by cyclin A/cyclin-dependent kinase 2 during the S-phase of the cell cycle and possesses both activator and repressor activities. It has been shown to activate the cell division cycle 2, cyclin D1, and insulin-like growth factor-binding protein 5 genes. Transcript variants may exist for this gene, but their full-length natures have not been determined.[1]

[edit] References

[edit] Further reading

  • Golay J, Cusmano G, Introna M (1992). "Independent regulation of c-myc, B-myb, and c-myb gene expression by inducers and inhibitors of proliferation in human B lymphocytes.". J. Immunol. 149 (1): 300–8. PMID 1376749. 
  • Reiss K, Travali S, Calabretta B, Baserga R (1991). "Growth regulated expression of B-myb in fibroblasts and hematopoietic cells.". J. Cell. Physiol. 148 (3): 338–43. doi:10.1002/jcp.1041480303. PMID 1717494. 
  • Golay J, Capucci A, Arsura M, et al. (1991). "Expression of c-myb and B-myb, but not A-myb, correlates with proliferation in human hematopoietic cells.". Blood 77 (1): 149–58. PMID 1984793. 
  • Nomura N, Takahashi M, Matsui M, et al. (1989). "Isolation of human cDNA clones of myb-related genes, A-myb and B-myb.". Nucleic Acids Res. 16 (23): 11075–89. PMID 3060855. 
  • Lam EW, Bennett JD, Watson RJ (1995). "Cell-cycle regulation of human B-myb transcription.". Gene 160 (2): 277–81. PMID 7642110. 
  • Takemoto Y, Tashiro S, Handa H, Ishii S (1994). "Multiple nuclear localization signals of the B-myb gene product.". FEBS Lett. 350 (1): 55–60. PMID 8062924. 
  • Zhou W, Takuwa N, Kumada M, Takuwa Y (1994). "E2F1, B-myb and selective members of cyclin/cdk subunits are targets for protein kinase C-mediated bimodal growth regulation in vascular endothelial cells.". Biochem. Biophys. Res. Commun. 199 (1): 191–8. doi:10.1006/bbrc.1994.1213. PMID 8123011. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • Arsura M, Luchetti MM, Erba E, et al. (1994). "Dissociation between p93B-myb and p75c-myb expression during the proliferation and differentiation of human myeloid cell lines.". Blood 83 (7): 1778–90. PMID 8142646. 
  • Nakagoshi H, Takemoto Y, Ishii S (1993). "Functional domains of the human B-myb gene product.". J. Biol. Chem. 268 (19): 14161–7. PMID 8314782. 
  • Noben-Trauth K, Copeland NG, Gilbert DJ, et al. (1996). "Mybl2 (Bmyb) maps to mouse chromosome 2 and human chromosome 20q 13.1.". Genomics 35 (3): 610–2. doi:10.1006/geno.1996.0408. PMID 8812502. 
  • Sala A, Kundu M, Casella I, et al. (1997). "Activation of human B-MYB by cyclins.". Proc. Natl. Acad. Sci. U.S.A. 94 (2): 532–6. PMID 9012818. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. 
  • Saville MK, Watson RJ (1998). "The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties.". Oncogene 17 (21): 2679–89. doi:10.1038/sj.onc.1202503. PMID 9840932. 
  • Bartsch O, Horstmann S, Toprak K, et al. (1999). "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb.". Eur. J. Biochem. 260 (2): 384–91. PMID 10095772. 
  • Kim T, Jung H, Min S, et al. (1999). "B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region.". FEBS Lett. 460 (2): 363–8. PMID 10544265. 
  • Johnson TK, Schweppe RE, Septer J, Lewis RE (2000). "Phosphorylation of B-Myb regulates its transactivation potential and DNA binding.". J. Biol. Chem. 274 (51): 36741–9. PMID 10593981. 
  • Horstmann S, Ferrari S, Klempnauer KH (2000). "Regulation of B-Myb activity by cyclin D1.". Oncogene 19 (2): 298–306. doi:10.1038/sj.onc.1203302. PMID 10645009. 
  • De Falco G, Bagella L, Claudio PP, et al. (2000). "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation.". Oncogene 19 (3): 373–9. doi:10.1038/sj.onc.1203305. PMID 10656684. 
  • Cervellera MN, Sala A (2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator.". J. Biol. Chem. 275 (14): 10692–6. PMID 10744766. 

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.