MYBL2

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V-myb avian myeloblastosis viral oncogene homolog-like 2
Protein MYBL2 PDB 1a5j.png
PDB rendering based on 1a5j.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MYBL2 ; B-MYB; BMYB
External IDs OMIM601415 MGI101785 HomoloGene1847 GeneCards: MYBL2 Gene
Orthologs
Species Human Mouse
Entrez 4605 17865
Ensembl ENSG00000101057 ENSMUSG00000017861
UniProt P10244 P48972
RefSeq (mRNA) NM_001278610 NM_008652
RefSeq (protein) NP_001265539 NP_032678
Location (UCSC) Chr 20:
42.3 – 42.35 Mb
Chr 2:
163.05 – 163.08 Mb
PubMed search [1] [2]

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[edit]

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]

References[edit]

  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. doi:10.1006/geno.1996.0408. PMID 8812502. 
  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. doi:10.1074/jbc.M308953200. ISSN 0021-9258. PMID 12947099. 
  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. doi:10.1038/sj.onc.1206001. ISSN 0950-9232. PMID 12439743. 
  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. doi:10.1182/blood.V97.7.2091. ISSN 0006-4971. PMID 11264149. 
  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. doi:10.1074/jbc.M105112200. ISSN 0021-9258. PMID 11733503. 
  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. doi:10.1038/sj.onc.1204439. ISSN 0950-9232. PMID 11423988. 
  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. doi:10.1038/sj.onc.1203305. ISSN 0950-9232. PMID 10656684. 
  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. doi:10.1074/jbc.275.14.10692. ISSN 0021-9258. PMID 10744766. 

Further reading[edit]

  • 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. doi:10.1093/nar/16.23.11075. PMC 338997. PMID 3060855. 
  • Lam EW, Bennett JD, Watson RJ (1995). "Cell-cycle regulation of human B-myb transcription". Gene 160 (2): 277–81. doi:10.1016/0378-1119(95)00184-8. 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. doi:10.1016/0014-5793(94)00733-0. 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. doi:10.1016/0378-1119(94)90802-8. 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. 
  • 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. doi:10.1073/pnas.94.2.532. PMC 19547. 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1046/j.1432-1327.1999.00191.x. 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. doi:10.1016/S0014-5793(99)01375-7. 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. doi:10.1074/jbc.274.51.36741. 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. doi:10.1074/jbc.275.14.10692. PMID 10744766. 

External links[edit]

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