Biology:MYBL2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Myb-related protein B is a protein that in humans is encoded by the MYBL2 gene.[1]
Function
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] MYBL2 is deregulated in various cancer types and can contribute to cancer progression.[3][4]
Interactions
MYBL2 has been shown to interact with:
- CDK9[5]
- CREB-binding protein[6]
- Cyclin A1[7]
- Cyclin-dependent kinase inhibitor 1C[8]
- EP300[9]
- PARP1[10]
- Retinoblastoma-like protein 1[8][11]
References
- ↑ "Mybl2 (Bmyb) maps to mouse chromosome 2 and human chromosome 20q 13.1". Genomics 35 (3): 610–2. August 1996. doi:10.1006/geno.1996.0408. PMID 8812502. https://zenodo.org/record/1229699.
- ↑ "Entrez Gene: MYBL2 v-myb myeloblastosis viral oncogene homolog (avian)-like 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4605.
- ↑ "MYBL2 (B-Myb): a central regulator of cell proliferation, cell survival and differentiation involved in tumorigenesis". Cell Death & Disease 8 (6): e2895. June 2017. doi:10.1038/cddis.2017.244. PMID 28640249.
- ↑ "Cooperation of cancer drivers with regulatory germline variants shapes clinical outcomes". Nature Communications 10 (1): 4128. September 2019. doi:10.1038/s41467-019-12071-2. PMID 31511524. Bibcode: 2019NatCo..10.4128M.
- ↑ "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene 19 (3): 373–9. January 2000. doi:10.1038/sj.onc.1203305. PMID 10656684.
- ↑ "Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator". Oncogene 20 (26): 3376–86. June 2001. doi:10.1038/sj.onc.1204439. PMID 11423988.
- ↑ "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 97 (7): 2091–7. April 2001. doi:10.1182/blood.V97.7.2091. PMID 11264176.
- ↑ 8.0 8.1 "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". The Journal of Biological Chemistry 278 (45): 44255–64. November 2003. doi:10.1074/jbc.M308953200. PMID 12947099.
- ↑ "Effects of B-Myb on gene transcription: phosphorylation-dependent activity and acetylation by p300". The Journal of Biological Chemistry 277 (6): 4088–97. February 2002. doi:10.1074/jbc.M105112200. PMID 11733503.
- ↑ "Poly(ADP-ribose) polymerase is a B-MYB coactivator". The Journal of Biological Chemistry 275 (14): 10692–6. April 2000. doi:10.1074/jbc.275.14.10692. PMID 10744766.
- ↑ "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene 21 (52): 7923–32. November 2002. doi:10.1038/sj.onc.1206001. PMID 12439743.
Further reading
- "Independent regulation of c-myc, B-myb, and c-myb gene expression by inducers and inhibitors of proliferation in human B lymphocytes". Journal of Immunology 149 (1): 300–8. July 1992. doi:10.4049/jimmunol.149.1.300. PMID 1376749.
- "Growth regulated expression of B-myb in fibroblasts and hematopoietic cells". Journal of Cellular Physiology 148 (3): 338–43. September 1991. doi:10.1002/jcp.1041480303. PMID 1717494.
- "Expression of c-myb and B-myb, but not A-myb, correlates with proliferation in human hematopoietic cells". Blood 77 (1): 149–58. January 1991. doi:10.1182/blood.V77.1.149.149. PMID 1984793.
- "Isolation of human cDNA clones of myb-related genes, A-myb and B-myb". Nucleic Acids Research 16 (23): 11075–89. December 1988. doi:10.1093/nar/16.23.11075. PMID 3060855.
- "Cell-cycle regulation of human B-myb transcription". Gene 160 (2): 277–81. July 1995. doi:10.1016/0378-1119(95)00184-8. PMID 7642110.
- "Multiple nuclear localization signals of the B-myb gene product". FEBS Letters 350 (1): 55–60. August 1994. doi:10.1016/0014-5793(94)00733-0. PMID 8062924.
- "E2F1, B-myb and selective members of cyclin/cdk subunits are targets for protein kinase C-mediated bimodal growth regulation in vascular endothelial cells". Biochemical and Biophysical Research Communications 199 (1): 191–8. February 1994. doi:10.1006/bbrc.1994.1213. PMID 8123011.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Dissociation between p93B-myb and p75c-myb expression during the proliferation and differentiation of human myeloid cell lines". Blood 83 (7): 1778–90. April 1994. doi:10.1182/blood.V83.7.1778.1778. PMID 8142646.
- "Functional domains of the human B-myb gene product". The Journal of Biological Chemistry 268 (19): 14161–7. July 1993. doi:10.1016/S0021-9258(19)85222-5. PMID 8314782.
- "Activation of human B-MYB by cyclins". Proceedings of the National Academy of Sciences of the United States of America 94 (2): 532–6. January 1997. doi:10.1073/pnas.94.2.532. PMID 9012818. Bibcode: 1997PNAS...94..532S.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "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. November 1998. doi:10.1038/sj.onc.1202503. PMID 9840932.
- "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb". European Journal of Biochemistry 260 (2): 384–91. March 1999. doi:10.1046/j.1432-1327.1999.00191.x. PMID 10095772.
- "B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region". FEBS Letters 460 (2): 363–8. October 1999. doi:10.1016/S0014-5793(99)01375-7. PMID 10544265.
- "Phosphorylation of B-Myb regulates its transactivation potential and DNA binding". The Journal of Biological Chemistry 274 (51): 36741–9. December 1999. doi:10.1074/jbc.274.51.36741. PMID 10593981.
- "Regulation of B-Myb activity by cyclin D1". Oncogene 19 (2): 298–306. January 2000. doi:10.1038/sj.onc.1203302. PMID 10645009.
- "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene 19 (3): 373–9. January 2000. doi:10.1038/sj.onc.1203305. PMID 10656684.
- "Poly(ADP-ribose) polymerase is a B-MYB coactivator". The Journal of Biological Chemistry 275 (14): 10692–6. April 2000. doi:10.1074/jbc.275.14.10692. PMID 10744766.
External links
- MYBL2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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