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MYBL2

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens
MYBL2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2D9A

Identifiers
AliasesMYBL2, B-MYB, BMYB, MYB proto-oncogene like 2
External IDsOMIM:601415;MGI:101785;HomoloGene:1847;GeneCards:MYBL2;OMA:MYBL2 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for MYBL2
Genomic location for MYBL2
Band20q13.12Start43,667,019bp[1]
End43,716,495bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for MYBL2
Genomic location for MYBL2
Band2 H2|2 84.0 cMStart162,896,607bp[2]
End162,926,608bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • ganglionic eminence

  • ventricular zone

  • beta cell

  • bone marrow

  • bone marrow cell

  • 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
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 2: 162.9 – 162.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myb-related protein B is aprotein that in humans is encoded by theMYBL2gene.[5]

Function

[edit]

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

[edit]

MYBL2 has been shown tointeract with:

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000101057Ensembl, May 2017
  2. ^abcGRCm38: 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.hdl:11380/15896.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. ^abJoaquin 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

[edit]

External links

[edit]

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

PDB gallery
  • 1a5j: CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES
    1a5j: CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES
  • 2d9a: Solution Structure of RSGI RUH-050, a myb DNA-binding domain in mouse cDNA
    2d9a: Solution Structure of RSGI RUH-050, a myb DNA-binding domain in mouse cDNA
(1) Basic domains
(1.1) Basicleucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3)bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2)Zinc finger DNA-binding domains
(2.1)Nuclear receptor(Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3.1)Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3)Fork head /winged helix
(3.4)Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4)β-Scaffold factors with minor groove contacts
(4.1)Rel homology region
(4.2)STAT
(4.3) p53-like
(4.4)MADS box
(4.6)TATA-binding proteins
(4.7)High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3)Pocket domain
(0.5)AP-2/EREBP-related factors
(0.6) Miscellaneous
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