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Title: Mybl2  
Author: World Heritage Encyclopedia
Language: English
Subject: Retinoblastoma-like protein 1, Cyclin-dependent kinase inhibitor 1C, Cyclin A1, Cyclin-dependent kinase 9, Transcription factors
Collection: Transcription Factors
Publisher: World Heritage Encyclopedia


V-myb avian myeloblastosis viral oncogene homolog-like 2

PDB rendering based on 1a5j.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; B-MYB; BMYB
External IDs GeneCards:
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Myb-related protein B is a protein that in humans is encoded by the MYBL2 gene.[1] 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.[2]


  • Interactions 1
  • References 2
  • Further reading 3
  • External links 4


MYBL2 has been shown to interact with Retinoblastoma-like protein 1,[3][4] Cyclin A1,[5] EP300,[6] CREB-binding protein,[7] CDK9,[8] Cyclin-dependent kinase inhibitor 1C[3] and PARP1.[9]


  1. ^ Noben-Trauth K, Copeland NG, Gilbert DJ, Jenkins NA, Sonoda G, Testa JR, Klempnauer KH (December 1996). "Mybl2 (Bmyb) maps to mouse chromosome 2 and human chromosome 20q 13.1". Genomics 35 (3): 610–2.  
  2. ^ "Entrez Gene: MYBL2 v-myb myeloblastosis viral oncogene homolog (avian)-like 2". 
  3. ^ a b Joaquin, Manel; Watson Roger J (November 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". J. Biol. Chem. (United States) 278 (45): 44255–64.  
  4. ^ Joaquin, Manel; Bessa Maria; Saville Mark K; Watson Roger J (November 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene (England) 21 (52): 7923–32.  
  5. ^ Müller-Tidow, C; Wang W, Idos G E, Diederichs S, Yang R, Readhead C, Berdel W E, Serve H, Saville M, Watson R, Koeffler H P (April 2001). "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function". Blood (United States) 97 (7): 2091–7.  
  6. ^ Johnson, Lance R; Johnson Teresa K; Desler Michelle; Luster Troy A; Nowling Tamara; Lewis Robert E; Rizzino Angie (February 2002). "Effects of B-Myb on gene transcription: phosphorylation-dependent activity ans acetylation by p300". J. Biol. Chem. (United States) 277 (6): 4088–97.  
  7. ^ Bessa, M; Saville M K; Watson R J (June 2001). "Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator". Oncogene (England) 20 (26): 3376–86.  
  8. ^ De Falco, G; Bagella L; Claudio P P; De Luca A; Fu Y; Calabretta B; Sala A; Giordano A (January 2000). "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene (ENGLAND) 19 (3): 373–9.  
  9. ^ Cervellera, M N; Sala A (April 2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator". J. Biol. Chem. (UNITED STATES) 275 (14): 10692–6.  

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.  
  • 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.  
  • 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.  
  • 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.  
  • Lam EW, Bennett JD, Watson RJ (1995). "Cell-cycle regulation of human B-myb transcription". Gene 160 (2): 277–81.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Nakagoshi H, Takemoto Y, Ishii S (1993). "Functional domains of the human B-myb gene product". J. Biol. Chem. 268 (19): 14161–7.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Horstmann S, Ferrari S, Klempnauer KH (2000). "Regulation of B-Myb activity by cyclin D1". Oncogene 19 (2): 298–306.  
  • 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.  
  • Cervellera MN, Sala A (2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator". J. Biol. Chem. 275 (14): 10692–6.  

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