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MYBL2

From Wikipedia, the free encyclopedia

MYBL2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMYBL2, B-MYB, BMYB, MYB proto-oncogene like 2
External IDsOMIM: 601415; MGI: 101785; HomoloGene: 1847; GeneCards: MYBL2; OMA:MYBL2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002466
NM_001278610

NM_008652

RefSeq (protein)

NP_001265539
NP_002457

NP_032678

Location (UCSC)Chr 20: 43.67 – 43.72 MbChr 2: 162.9 – 162.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function

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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

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MYBL2 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101057Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017861Ensembl, 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. ^ a b 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

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