YY1

Last updated

YY1
Protein YY1 PDB 1ubd.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases YY1 , DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, YY1 transcription factor, GADEVS
External IDs OMIM: 600013; MGI: 99150; HomoloGene: 2556; GeneCards: YY1; OMA:YY1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003403

NM_009537

RefSeq (protein)

NP_003394

NP_033563

Location (UCSC) Chr 14: 100.24 – 100.28 Mb Chr 12: 108.76 – 108.79 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

YY1 (Yin Yang 1) [5] is a transcriptional repressor protein in humans that is encoded by the YY1 gene. [6] [7]

Contents

Function

YY1 is a ubiquitously distributed transcription factor belonging to the GLI-Kruppel class of zinc finger proteins. The protein is involved in repressing and activating a diverse number of promoters. Hence, the YY in the name stands for "yin-yang." YY1 may direct histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter, thus implicating histone modification in the function of YY1. [8] YY1 promotes enhancer-promoter chromatin loops by forming dimers and promoting DNA interactions. Its dysregulation disrupts enhancer-promoter loops and gene expression. [9] [10]

Clinical significance

YY1 heterozygous deletions, missense, and nonsense mutations cause Gabriele-DeVries syndrome (GADEVS), [11] [12] an autosomal dominant neurodevelopmental disorder characterized by intellectual disability, dysmorphic facial features, feeding problems, intrauterine growth restriction, variable cognitive impairment, behavioral problems and other congenital malformations. [10] A website is available in order to collect and share clinical information between clinicians and the families of affected individuals. [13]

Interactions

YY1 has been shown to interact with:

Related Research Articles

In molecular biology and genetics, transcriptional regulation is the means by which a cell regulates the conversion of DNA to RNA (transcription), thereby orchestrating gene activity. A single gene can be regulated in a range of ways, from altering the number of copies of RNA that are transcribed, to the temporal control of when the gene is transcribed. This control allows the cell or organism to respond to a variety of intra- and extracellular signals and thus mount a response. Some examples of this include producing the mRNA that encode enzymes to adapt to a change in a food source, producing the gene products involved in cell cycle specific activities, and producing the gene products responsible for cellular differentiation in multicellular eukaryotes, as studied in evolutionary developmental biology.

<span class="mw-page-title-main">Histone deacetylase</span> Class of enzymes important in regulating DNA transcription

Histone deacetylases (EC 3.5.1.98, HDAC) are a class of enzymes that remove acetyl groups (O=C-CH3) from an ε-N-acetyl lysine amino acid on both histone and non-histone proteins. HDACs allow histones to wrap the DNA more tightly. This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. HDAC's action is opposite to that of histone acetyltransferase. HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins. In general, they suppress gene expression.

<span class="mw-page-title-main">HDAC1</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 1 (HDAC1) is an enzyme that in humans is encoded by the HDAC1 gene.

<span class="mw-page-title-main">Histone deacetylase 2</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 2 (HDAC2) is an enzyme that in humans is encoded by the HDAC2 gene. It belongs to the histone deacetylase class of enzymes responsible for the removal of acetyl groups from lysine residues at the N-terminal region of the core histones. As such, it plays an important role in gene expression by facilitating the formation of transcription repressor complexes and for this reason is often considered an important target for cancer therapy.

<span class="mw-page-title-main">HDAC3</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 3 is an enzyme encoded by the HDAC3 gene in both humans and mice.

<span class="mw-page-title-main">SIN3A</span> Protein-coding gene in the species Homo sapiens

Paired amphipathic helix protein Sin3a is a protein that in humans is encoded by the SIN3A gene.

<span class="mw-page-title-main">HDAC4</span>

Histone deacetylase 4, also known as HDAC4, is a protein that in humans is encoded by the HDAC4 gene.

<span class="mw-page-title-main">TRIM28</span> Protein-coding gene in the species Homo sapiens

Tripartite motif-containing 28 (TRIM28), also known as transcriptional intermediary factor 1β (TIF1β) and KAP1, is a protein that in humans is encoded by the TRIM28 gene.

<span class="mw-page-title-main">CTBP1</span> Protein-coding gene in the species Homo sapiens

C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene. CtBP1 is one of two CtBP proteins, the other protein being CtBP2.

<span class="mw-page-title-main">Myocyte-specific enhancer factor 2A</span> Protein-coding gene in the species Homo sapiens

Myocyte-specific enhancer factor 2A is a protein that in humans is encoded by the MEF2A gene. MEF2A is a transcription factor in the Mef2 family. In humans it is located on chromosome 15q26. Certain mutations in MEF2A cause an autosomal dominant form of coronary artery disease and myocardial infarction.

<span class="mw-page-title-main">Histone deacetylase 5</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 5 is an enzyme that in humans is encoded by the HDAC5 gene.

<span class="mw-page-title-main">HDAC9</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 9 is an enzyme that in humans is encoded by the HDAC9 gene.

<span class="mw-page-title-main">MEF2D</span> Protein-coding gene in the species Homo sapiens

Myocyte-specific enhancer factor 2D is a protein that in humans is encoded by the MEF2D gene.

<span class="mw-page-title-main">TFCP2</span> Protein-coding gene in the species Homo sapiens

Alpha-globin transcription factor CP2 is a protein that in humans is encoded by the TFCP2 gene.

<span class="mw-page-title-main">SAP30</span> Protein-coding gene in the species Homo sapiens

Sin3A-associated protein, 30kDa, also known as SAP30, is a protein which in humans is encoded by the SAP30 gene.

<span class="mw-page-title-main">CTBP2</span> Protein-coding gene in the species Homo sapiens

C-terminal-binding protein 2 also known as CtBP2 is a protein that in humans is encoded by the CTBP2 gene.

<span class="mw-page-title-main">SIN3B</span> Protein-coding gene in the species Homo sapiens

Paired amphipathic helix protein Sin3b is a protein that in humans is encoded by the SIN3B gene.

<span class="mw-page-title-main">FKBP3</span> Protein-coding gene in the species Homo sapiens

FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene.

<span class="mw-page-title-main">Sp2 transcription factor</span> Protein-coding gene in the species Homo sapiens

Transcription factor Sp2 is a protein that in humans is encoded by the SP2 gene.

<span class="mw-page-title-main">ARID4A</span> Protein-coding gene in humans

AT rich interactive domain 4A (RBP1-like), also known as ARID4A, is a protein which in humans is encoded by the ARID4A gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000100811 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000021264 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. Thiaville MM, Kim J (2011). "Oncogenic potential of yin yang 1 mediated through control of imprinted genes". Critical Reviews in Oncogenesis. 16 (3–4): 199–209. doi:10.1615/critrevoncog.v16.i3-4.40. PMC   3392609 . PMID   22248054.
  6. Shi Y, Seto E, Chang LS, Shenk T (October 1991). "Transcriptional repression by YY1, a human GLI-Krüppel-related protein, and relief of repression by adenovirus E1A protein". Cell. 67 (2): 377–88. doi:10.1016/0092-8674(91)90189-6. PMID   1655281. S2CID   19399858.
  7. Zhu W, Lossie AC, Camper SA, Gumucio DL (April 1994). "Chromosomal localization of the transcription factor YY1 in the mouse and human". Mammalian Genome. 5 (4): 234–6. doi:10.1007/BF00360552. hdl: 2027.42/47010 . PMID   7912122. S2CID   27296553.
  8. "Entrez Gene: YY1 YY1 transcription factor".
  9. Weintraub AS, Li CH, Zamudio AV, Sigova AA, Hannett NM, Day DS, et al. (December 2017). "YY1 Is a Structural Regulator of Enhancer-Promoter Loops". Cell. 171 (7): 1573–1588.e28. doi:10.1016/j.cell.2017.11.008. PMC   5785279 . PMID   29224777.
  10. 1 2 Gabriele M, Vulto-van Silfhout AT, Germain PL, Vitriolo A, Kumar R, Douglas E, et al. (June 2017). "YY1 Haploinsufficiency Causes an Intellectual Disability Syndrome Featuring Transcriptional and Chromatin Dysfunction". American Journal of Human Genetics. 100 (6): 907–925. doi:10.1016/j.ajhg.2017.05.006. PMC   5473733 . PMID   28575647.
  11. "Gabriele-de Vries Syndrome". OMIM.
  12. Nabais Sá MJ, Gabriele M, Testa G, de Vries BB (1993). "Gabriele-de Vries Syndrome". In Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE, Bean LJ, Gripp KW, Amemiya A (eds.). GeneReviews [Internet]. Seattle (WA): University of Washington, Seattle. PMID   31145572.
  13. "YY1 – Collect information about clinic management and research projects". YY1.
  14. Li M, Baumeister P, Roy B, Phan T, Foti D, Luo S, et al. (July 2000). "ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1". Molecular and Cellular Biology. 20 (14): 5096–106. doi:10.1128/mcb.20.14.5096-5106.2000. PMC   85959 . PMID   10866666.
  15. 1 2 3 Yao YL, Yang WM, Seto E (September 2001). "Regulation of transcription factor YY1 by acetylation and deacetylation". Molecular and Cellular Biology. 21 (17): 5979–91. doi:10.1128/mcb.21.17.5979-5991.2001. PMC   87316 . PMID   11486036.
  16. Lee JS, Galvin KM, See RH, Eckner R, Livingston D, Moran E, et al. (May 1995). "Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300". Genes & Development. 9 (10): 1188–98. doi: 10.1101/gad.9.10.1188 . PMID   7758944.
  17. Yang WM, Yao YL, Seto E (September 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". The EMBO Journal. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC   125595 . PMID   11532945.
  18. 1 2 Yang WM, Yao YL, Sun JM, Davie JR, Seto E (October 1997). "Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family". The Journal of Biological Chemistry. 272 (44): 28001–7. doi: 10.1074/jbc.272.44.28001 . PMID   9346952.
  19. Kalenik JL, Chen D, Bradley ME, Chen SJ, Lee TC (February 1997). "Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1". Nucleic Acids Research. 25 (4): 843–9. doi:10.1093/nar/25.4.843. PMC   146511 . PMID   9016636.
  20. Shrivastava A, Saleque S, Kalpana GV, Artandi S, Goff SP, Calame K (December 1993). "Inhibition of transcriptional regulator Yin-Yang-1 by association with c-Myc". Science. 262 (5141): 1889–92. Bibcode:1993Sci...262.1889S. doi:10.1126/science.8266081. PMID   8266081.
  21. Yeh TS, Lin YM, Hsieh RH, Tseng MJ (October 2003). "Association of transcription factor YY1 with the high molecular weight Notch complex suppresses the transactivation activity of Notch". The Journal of Biological Chemistry. 278 (43): 41963–9. doi: 10.1074/jbc.M304353200 . PMID   12913000.
  22. García E, Marcos-Gutiérrez C, del Mar Lorente M, Moreno JC, Vidal M (June 1999). "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1". The EMBO Journal. 18 (12): 3404–18. doi:10.1093/emboj/18.12.3404. PMC   1171420 . PMID   10369680.
  23. Huang NE, Lin CH, Lin YS, Yu WC (June 2003). "Modulation of YY1 activity by SAP30". Biochemical and Biophysical Research Communications. 306 (1): 267–75. doi:10.1016/s0006-291x(03)00966-5. PMID   12788099.
  24. Fu CY, Wang P, Tsai HJ (November 2017). "Competitive binding between Seryl-tRNA synthetase/YY1 complex and NFKB1 at the distal segment results in differential regulation of human vegfa promoter activity during angiogenesis". Nucleic Acids Research. 45 (5): 2423–2437. doi:10.1093/nar/gkw1187. PMC   5389716 . PMID   27913726.

Further reading