MYBL2

MYBL2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2D9A
Identifiers
Aliases	MYBL2, B-MYB, BMYB, MYB proto-oncogene like 2
External IDs	OMIM: 601415; MGI: 101785; HomoloGene: 1847; GeneCards: MYBL2; OMA:MYBL2 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) Band 20q13.12 Start 43,667,019 bp End 43,716,495 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 H2|2 84.0 cM Start 162,896,607 bp End 162,926,608 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad ganglionic eminence ventricular zone beta cell bone marrow bone marrow cells appendix mucosa of transverse colon lymph node trabecular bone Top expressed in zygote yolk sac secondary oocyte blastocyst primary oocyte morula epiblast female urethra tail of embryo embryo More reference expression data BioGPS n/a
Gene ontology Molecular function RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific protein binding DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component Myb complex nucleoplasm nucleus Biological process regulation of cell cycle regulation of transcription, DNA-templated transcription, DNA-templated positive regulation of transcription by RNA polymerase II transcription by RNA polymerase II cell differentiation mitotic spindle assembly regulation of transcription by RNA polymerase II positive regulation of neuron apoptotic process cellular response to leukemia inhibitory factor mitotic cell cycle positive regulation of transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4605 17865 Ensembl ENSG00000101057 ENSMUSG00000017861 UniProt P10244 P48972 RefSeq (mRNA) NM_002466 NM_001278610 NM_008652 RefSeq (protein) NP_001265539 NP_002457 NP_032678 Location (UCSC) Chr 20: 43.67 – 43.72 Mb Chr 2: 162.9 – 162.93 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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. MYBL2 is deregulated in various cancer types and can contribute to cancer progression.

Interactions

MYBL2 has been shown to interact with:

• CDK9
• CREB-binding protein
• Cyclin A1
• Cyclin-dependent kinase inhibitor 1C
• EP300
• PARP1
• Retinoblastoma-like protein 1

Further reading

• Golay J, Cusmano G, Introna M (July 1992). "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. doi:10.4049/jimmunol.149.1.300. PMID 1376749.
• Reiss K, Travali S, Calabretta B, Baserga R (September 1991). "Growth regulated expression of B-myb in fibroblasts and hematopoietic cells". Journal of Cellular Physiology. 148 (3): 338–43. doi:10.1002/jcp.1041480303. PMID 1717494. S2CID 30389377.
• Golay J, Capucci A, Arsura M, Castellano M, Rizzo V, Introna M (January 1991). "Expression of c-myb and B-myb, but not A-myb, correlates with proliferation in human hematopoietic cells". Blood. 77 (1): 149–58. doi:10.1182/blood.V77.1.149.149. PMID 1984793.
• Nomura N, Takahashi M, Matsui M, Ishii S, Date T, Sasamoto S, Ishizaki R (December 1988). "Isolation of human cDNA clones of myb-related genes, A-myb and B-myb". Nucleic Acids Research. 16 (23): 11075–89. doi:10.1093/nar/16.23.11075. PMC 338997. PMID 3060855.
• Lam EW, Bennett JD, Watson RJ (July 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 (August 1994). "Multiple nuclear localization signals of the B-myb gene product". FEBS Letters. 350 (1): 55–60. Bibcode:1994FEBSL.350...55T. doi:10.1016/0014-5793(94)00733-0. PMID 8062924. S2CID 45799740.
• Zhou W, Takuwa N, Kumada M, Takuwa Y (February 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". Biochemical and Biophysical Research Communications. 199 (1): 191–8. doi:10.1006/bbrc.1994.1213. PMID 8123011.
• Maruyama K, Sugano S (January 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, Golay J, Rambaldi A, Introna M (April 1994). "Dissociation between p93B-myb and p75c-myb expression during the proliferation and differentiation of human myeloid cell lines". Blood. 83 (7): 1778–90. doi:10.1182/blood.V83.7.1778.1778. PMID 8142646.
• Nakagoshi H, Takemoto Y, Ishii S (July 1993). "Functional domains of the human B-myb gene product". The Journal of Biological Chemistry. 268 (19): 14161–7. doi:10.1016/S0021-9258(19)85222-5. PMID 8314782.
• Sala A, Kundu M, Casella I, Engelhard A, Calabretta B, Grasso L, et al. (January 1997). "Activation of human B-MYB by cyclins". Proceedings of the National Academy of Sciences of the United States of America. 94 (2): 532–6. Bibcode:1997PNAS...94..532S. doi:10.1073/pnas.94.2.532. PMC 19547. PMID 9012818.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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 (November 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. S2CID 23576308.
• Bartsch O, Horstmann S, Toprak K, Klempnauer KH, Ferrari S (March 1999). "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb". European Journal of Biochemistry. 260 (2): 384–91. doi:10.1046/j.1432-1327.1999.00191.x. PMID 10095772.
• Kim T, Jung H, Min S, Kim KT, Ha H (October 1999). "B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region". FEBS Letters. 460 (2): 363–8. Bibcode:1999FEBSL.460..363K. doi:10.1016/S0014-5793(99)01375-7. PMID 10544265. S2CID 36560086.
• Johnson TK, Schweppe RE, Septer J, Lewis RE (December 1999). "Phosphorylation of B-Myb regulates its transactivation potential and DNA binding". The Journal of Biological Chemistry. 274 (51): 36741–9. doi:10.1074/jbc.274.51.36741. PMID 10593981.
• Horstmann S, Ferrari S, Klempnauer KH (January 2000). "Regulation of B-Myb activity by cyclin D1". Oncogene. 19 (2): 298–306. doi:10.1038/sj.onc.1203302. PMID 10645009. S2CID 8417008.
• De Falco G, Bagella L, Claudio PP, De Luca A, Fu Y, Calabretta B, et al. (January 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 (April 2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator". The Journal of Biological Chemistry. 275 (14): 10692–6. doi:10.1074/jbc.275.14.10692. PMID 10744766.

External links

• MYBL2+protein,+human at the U.S. 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.