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MYBL2 has been shown to [[Protein-protein interaction|interact]] with:
MYBL2 has been shown to [[Protein-protein interaction|interact]] with:
* [[CDK9]],<ref name = pmid10656684>{{cite journal | vauthors = De Falco G, Bagella L, Claudio PP, De Luca A, Fu Y, Calabretta B, Sala A, Giordano A | title = Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation | journal = Oncogene | volume = 19 | issue = 3 | pages = 373–9 | date = Jan 2000 | pmid = 10656684 | doi = 10.1038/sj.onc.1203305 }}</ref>  
* [[CDK9]]<ref name = pmid10656684>{{cite journal | vauthors = De Falco G, Bagella L, Claudio PP, De Luca A, Fu Y, Calabretta B, Sala A, Giordano A | title = Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation | journal = Oncogene | volume = 19 | issue = 3 | pages = 373–9 | date = Jan 2000 | pmid = 10656684 | doi = 10.1038/sj.onc.1203305 }}</ref>
* [[CREB-binding protein]],<ref name = pmid11423988>{{cite journal | vauthors = Bessa M, Saville MK, Watson RJ | title = Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator | journal = Oncogene | volume = 20 | issue = 26 | pages = 3376–86 | date = Jun 2001 | pmid = 11423988 | doi = 10.1038/sj.onc.1204439 }}</ref>  
* [[CREB-binding protein]]<ref name = pmid11423988>{{cite journal | vauthors = Bessa M, Saville MK, Watson RJ | title = Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator | journal = Oncogene | volume = 20 | issue = 26 | pages = 3376–86 | date = Jun 2001 | pmid = 11423988 | doi = 10.1038/sj.onc.1204439 }}</ref>
* [[Cyclin A1]],<ref name = pmid11264176>{{cite journal | vauthors =Müller-Tidow C, Wang W, Idos GE, Diederichs S, Yang R, Readhead C, Berdel WE, Serve H, Saville M, Watson R, Koeffler HP  | title =  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| journal =  Blood| volume =  97| issue =  | date = April 2001 | pmid = 11264176 | doi = 10.1182/blood.V97.7.2091 | pages=2091–7}}</ref>  
* [[Cyclin A1]]<ref name = pmid11264176>{{cite journal | vauthors =Müller-Tidow C, Wang W, Idos GE, Diederichs S, Yang R, Readhead C, Berdel WE, Serve H, Saville M, Watson R, Koeffler HP  | title =  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| journal =  Blood| volume =  97| issue =  | date = April 2001 | pmid = 11264176 | doi = 10.1182/blood.V97.7.2091 | pages=2091–7}}</ref>
* [[Cyclin-dependent kinase inhibitor 1C]]<ref name = pmid12947099/>  
* [[Cyclin-dependent kinase inhibitor 1C]]<ref name = pmid12947099/>  
* [[EP300]],<ref name = pmid11733503>{{cite journal | vauthors = Johnson LR, Johnson TK, Desler M, Luster TA, Nowling T, Lewis RE, Rizzino A | title = Effects of B-Myb on gene transcription: phosphorylation-dependent activity and acetylation by p300 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 6 | pages = 4088–97 | date = Feb 2002 | pmid = 11733503 | doi = 10.1074/jbc.M105112200 }}</ref>  
* [[EP300]]<ref name = pmid11733503>{{cite journal | vauthors = Johnson LR, Johnson TK, Desler M, Luster TA, Nowling T, Lewis RE, Rizzino A | title = Effects of B-Myb on gene transcription: phosphorylation-dependent activity and acetylation by p300 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 6 | pages = 4088–97 | date = Feb 2002 | pmid = 11733503 | doi = 10.1074/jbc.M105112200 }}</ref>
* [[PARP1]],<ref name = pmid10744766>{{cite journal | vauthors = Cervellera MN, Sala A | title = Poly(ADP-ribose) polymerase is a B-MYB coactivator | journal = The Journal of Biological Chemistry | volume = 275 | issue = 14 | pages = 10692–6 | date = Apr 2000 | pmid = 10744766 | doi =  10.1074/jbc.275.14.10692}}</ref> and
* [[PARP1]]<ref name = pmid10744766>{{cite journal | vauthors = Cervellera MN, Sala A | title = Poly(ADP-ribose) polymerase is a B-MYB coactivator | journal = The Journal of Biological Chemistry | volume = 275 | issue = 14 | pages = 10692–6 | date = Apr 2000 | pmid = 10744766 | doi =  10.1074/jbc.275.14.10692}}</ref>
* [[Retinoblastoma-like protein 1]].<ref name = pmid12947099>{{cite journal | vauthors = Joaquin M, Watson RJ | title = The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain | journal = The Journal of Biological Chemistry | volume = 278 | issue = 45 | pages = 44255–64 | date = Nov 2003 | pmid = 12947099 | doi = 10.1074/jbc.M308953200 }}</ref><ref name = pmid12439743>{{cite journal | vauthors = Joaquin M, Bessa M, Saville MK, Watson RJ | title = B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107 | journal = Oncogene | volume = 21 | issue = 52 | pages = 7923–32 | date = Nov 2002 | pmid = 12439743 | doi = 10.1038/sj.onc.1206001 }}</ref>
* [[Retinoblastoma-like protein 1]]<ref name = pmid12947099>{{cite journal | vauthors = Joaquin M, Watson RJ | title = The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain | journal = The Journal of Biological Chemistry | volume = 278 | issue = 45 | pages = 44255–64 | date = Nov 2003 | pmid = 12947099 | doi = 10.1074/jbc.M308953200 }}</ref><ref name = pmid12439743>{{cite journal | vauthors = Joaquin M, Bessa M, Saville MK, Watson RJ | title = B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107 | journal = Oncogene | volume = 21 | issue = 52 | pages = 7923–32 | date = Nov 2002 | pmid = 12439743 | doi = 10.1038/sj.onc.1206001 }}</ref>


== References ==
== References ==

Latest revision as of 07:13, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

Interactions

MYBL2 has been shown to interact with:

References

  1. ↑ Noben-Trauth K, Copeland NG, Gilbert DJ, Jenkins NA, Sonoda G, Testa JR, Klempnauer KH (Aug 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.
  2. ↑ "Entrez Gene: MYBL2 v-myb myeloblastosis viral oncogene homolog (avian)-like 2".
  3. ↑ De Falco G, Bagella L, Claudio PP, De Luca A, Fu Y, Calabretta B, Sala A, Giordano A (Jan 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.
  4. ↑ Bessa M, Saville MK, Watson RJ (Jun 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.
  5. ↑ Müller-Tidow C, Wang W, Idos GE, Diederichs S, Yang R, Readhead C, Berdel WE, Serve H, Saville M, Watson R, Koeffler HP (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: 2091–7. doi:10.1182/blood.V97.7.2091. PMID 11264176.
  6. ↑ 6.0 6.1 Joaquin M, Watson RJ (Nov 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.
  7. ↑ Johnson LR, Johnson TK, Desler M, Luster TA, Nowling T, Lewis RE, Rizzino A (Feb 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.
  8. ↑ Cervellera MN, Sala A (Apr 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.
  9. ↑ Joaquin M, Bessa M, Saville MK, Watson RJ (Nov 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 (Jul 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 (Sep 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 (Jan 1991). "Expression of c-myb and B-myb, but not A-myb, correlates with proliferation in human hematopoietic cells". Blood. 77 (1): 149–58. PMID 1984793.
  • Nomura N, Takahashi M, Matsui M, Ishii S, Date T, Sasamoto S, Ishizaki R (Dec 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 (Jul 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 (Aug 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 (Feb 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 (Jan 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 (Apr 1994). "Dissociation between p93B-myb and p75c-myb expression during the proliferation and differentiation of human myeloid cell lines". Blood. 83 (7): 1778–90. PMID 8142646.
  • Nakagoshi H, Takemoto Y, Ishii S (Jul 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, Paggi MG, Giordano A, Watson RJ, Khalili K, Peschle C (Jan 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 (Oct 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 (Nov 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 (Mar 1999). "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb". European Journal of Biochemistry / FEBS. 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 (Oct 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 (Dec 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 (Jan 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, Sala A, Giordano A (Jan 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 (Apr 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

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

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