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
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 162,896,607 bp [2] End 162,926,608 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence bone marrow bone marrow cells appendix lymph node spongy bone spleen oocyte secondary oocyte stromal cell of endometrium Top expressed in yolk sac secondary oocyte morula female urethra pharynx spermatid male urethra maxillary prominence thymus primitive streak 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2019NatCo..10.4128M. 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 and 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. S2CID   21761703.

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. 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. 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.