MYBL2

Myb-related protein B is a protein that in humans is encoded by the MYBL2 gene.[5]

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
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q13.12 Start 43,667,019 bp[1] End 43,716,495 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 H2|2 84.0 cM Start 163,054,687 bp[2] End 163,084,688 bp[2]
Gene ontology Molecular function • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding • DNA binding • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific • GO:0001948 protein binding • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component • Myb complex • nucleoplasm • cell nucleus Biological process • regulation of cell cycle • regulation of transcription, DNA-templated • transcription, DNA-templated • positive regulation of transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • cell differentiation • mitotic spindle assembly • regulation of transcription from RNA polymerase II promoter • positive regulation of neuron apoptotic process • cellular response to leukemia inhibitory factor • GO:0007067 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: 163.05 – 163.08 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6] MYBL2 is deregulated in various cancer types and can contribute to cancer progression.[7][8]

Interactions

MYBL2 has been shown to interact with:

• CDK9[9]
• CREB-binding protein[10]
• Cyclin A1[11]
• Cyclin-dependent kinase inhibitor 1C[12]
• EP300[13]
• PARP1[14]
• Retinoblastoma-like protein 1[12][15]

References

1. GRCh38: Ensembl release 89: ENSG00000101057 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000017861 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Noben-Trauth K, Copeland NG, Gilbert DJ, Jenkins NA, Sonoda G, Testa JR, Klempnauer KH (August 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.
6. "Entrez Gene: MYBL2 v-myb myeloblastosis viral oncogene homolog (avian)-like 2".
7. Musa J, Aynaud MM, Mirabeau O, Delattre O, Grünewald TG (June 2017). "MYBL2 (B-Myb): a central regulator of cell proliferation, cell survival and differentiation involved in tumorigenesis". Cell Death & Disease. 8 (6): e2895. doi:10.1038/cddis.2017.244. PMC 5520903. PMID 28640249.
8. Musa J, Cidre-Aranaz F, Aynaud MM, Orth MF, Knott MM, Mirabeau O, et al. (September 2019). "Cooperation of cancer drivers with regulatory germline variants shapes clinical outcomes". Nature Communications. 10 (1): 4128. doi:10.1038/s41467-019-12071-2. PMC 6739408. PMID 31511524.
9. 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.
10. Bessa M, Saville MK, Watson RJ (June 2001). "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. doi:10.1038/sj.onc.1204439. PMID 11423988.
11. Müller-Tidow C, Wang W, Idos GE, Diederichs S, Yang R, Readhead C, et al. (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. 97 (7): 2091–7. doi:10.1182/blood.V97.7.2091. PMID 11264176.
12. Joaquin M, Watson RJ (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". The Journal of Biological Chemistry. 278 (45): 44255–64. doi:10.1074/jbc.M308953200. PMID 12947099.
13. Johnson LR, Johnson TK, Desler M, Luster TA, Nowling T, Lewis RE, Rizzino A (February 2002). "Effects of B-Myb on gene transcription: phosphorylation-dependent activity ans acetylation by p300". The Journal of Biological Chemistry. 277 (6): 4088–97. doi:10.1074/jbc.M105112200. PMID 11733503.
14. 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.
15. Joaquin M, Bessa M, Saville MK, Watson RJ (November 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene. 21 (52): 7923–32. doi:10.1038/sj.onc.1206001. PMID 12439743.

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. 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.
• 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. doi:10.1016/0014-5793(94)00733-0. PMID 8062924.
• 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. 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. 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.
• 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. doi:10.1016/S0014-5793(99)01375-7. PMID 10544265.
• 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.
• 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 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.