SUZ12

Last updated
SUZ12
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SUZ12 , CHET9, JJAZ1, SUZ12 polycomb repressive complex 2 subunit, polycomb repressive complex 2 subunit, IMMAS
External IDs OMIM: 606245 MGI: 1261758 HomoloGene: 32256 GeneCards: SUZ12
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_015355
NM_001321207

NM_001163018
NM_199196

RefSeq (protein)

NP_001308136
NP_056170

NP_001156490
NP_954666

Location (UCSC) Chr 17: 31.94 – 32 Mb Chr 11: 79.88 – 79.92 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Polycomb protein SUZ12 is a protein that in humans is encoded by the SUZ12 gene. [5] [6] [7] [8]

Contents

Function

This zinc finger gene has been identified at the breakpoints of a recurrent chromosomal translocation reported in endometrial stromal sarcoma. Recombination of these breakpoints results in the fusion of this gene and JAZF1. The protein encoded by this gene contains a zinc finger domain in the C terminus of the coding region. The specific function of this gene has not yet been determined. [8]

SUZ12, as part of Polycomb Repressive Complex 2 (PRC2), may be involved with chromatin silencing in conjunction with HOTAIR ncRNA, using its zinc-finger domain to bind the RNA molecule. [9]

Related Research Articles

<span class="mw-page-title-main">Histone</span> Family proteins package and order the DNA into structural units called nucleosomes.

In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei. They act as spools around which DNA winds to create structural units called nucleosomes. Nucleosomes in turn are wrapped into 30-nanometer fibers that form tightly packed chromatin. Histones prevent DNA from becoming tangled and protect it from DNA damage. In addition, histones play important roles in gene regulation and DNA replication. Without histones, unwound DNA in chromosomes would be very long. For example, each human cell has about 1.8 meters of DNA if completely stretched out; however, when wound about histones, this length is reduced to about 90 micrometers (0.09 mm) of 30 nm diameter chromatin fibers.

<span class="mw-page-title-main">Histone methyltransferase</span> Histone-modifying enzymes

Histone methyltransferases (HMT) are histone-modifying enzymes, that catalyze the transfer of one, two, or three methyl groups to lysine and arginine residues of histone proteins. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4. Two major types of histone methyltranferases exist, lysine-specific and arginine-specific. In both types of histone methyltransferases, S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.
The genomic DNA of eukaryotes associates with histones to form chromatin. The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones. Histone methylation is a principal epigenetic modification of chromatin that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.

<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">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">RBBP4</span> Protein-coding gene in the species Homo sapiens

Histone-binding protein RBBP4 is a protein that in humans is encoded by the RBBP4 gene.

<span class="mw-page-title-main">EZH2</span> Protein-coding gene in the species Homo sapiens

Enhancer of zeste homolog 2 (EZH2) is a histone-lysine N-methyltransferase enzyme encoded by EZH2 gene, that participates in histone methylation and, ultimately, transcriptional repression. EZH2 catalyzes the addition of methyl groups to histone H3 at lysine 27, by using the cofactor S-adenosyl-L-methionine. Methylation activity of EZH2 facilitates heterochromatin formation thereby silences gene function. Remodeling of chromosomal heterochromatin by EZH2 is also required during cell mitosis.

<span class="mw-page-title-main">Methyl-CpG-binding domain protein 2</span> Protein-coding gene in the species Homo sapiens

Methyl-CpG-binding domain protein 2 is a protein that in humans is encoded by the MBD2 gene.

<span class="mw-page-title-main">RBBP7</span> Protein-coding gene in the species Homo sapiens

Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 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">Polycomb protein EED</span> Protein-coding gene in the species Homo sapiens

Polycomb protein EED is a protein that in humans is encoded by the EED gene.

<span class="mw-page-title-main">PHC2</span> Protein-coding gene in the species Homo sapiens

Polyhomeotic-like protein 2 is a protein that in humans is encoded by the PHC2 gene.

<span class="mw-page-title-main">KDM2A</span> Protein-coding gene in the species Homo sapiens

Lysine-specific demethylase 2A (KDM2A) also known as F-box and leucine-rich repeat protein 11 (FBXL11) is an enzyme that in humans is encoded by the KDM2A gene. KDM2A is a member of the superfamily of alpha-ketoglutarate-dependent hydroxylases, which are non-haem iron-containing proteins.

<span class="mw-page-title-main">SETD7</span> Protein-coding gene in the species Homo sapiens

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.

<span class="mw-page-title-main">KMT5A</span>

N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene. The enzyme is a histone methyltransferase, SET domain-containing and lysine-specific. The enzyme transfers one methyl group to histone H4 lysine residue at position 20. S-Adenosyl methionine (SAM) is both the cofactor and the methyl group donor. The lysine residue is converted to N6-methyllysine residue.

<span class="mw-page-title-main">PRC2</span>

PRC2 is one of the two classes of polycomb-group proteins or (PcG). The other component of this group of proteins is PRC1.

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

The SET domain is a protein domain that typically has methyltransferase activity. It was originally identified as part of a larger conserved region present in the Drosophila Trithorax protein and was subsequently identified in the Drosophila Su(var)3-9 and 'Enhancer of zeste' proteins, from which the acronym SET is derived [Su(var)3-9, Enhancer-of-zeste and Trithorax].

<span class="mw-page-title-main">KDM2B</span>

The human KDM2B gene encodes the protein lysine (K)-specific demethylase 2B.

<span class="mw-page-title-main">Yi Zhang (biochemist)</span> Chinese-American biochemist

Yi Zhang is a Chinese-American biochemist who specializes in the fields of epigenetics, chromatin, and developmental reprogramming. He is a Fred Rosen Professor of Pediatrics and Professor of Genetics at Harvard Medical School, a Senior Investigator of Program in Cellular and Molecular Medicine at Boston Children's Hospital, and an Investigator of the Howard Hughes Medical Institute. He is also an Associate Member of the Harvard Stem Cell Institute, as well as the Broad Institute of MIT and Harvard. He is best known for his discovery of several classes of epigenetic enzymes and the identification of epigenetic barriers of SCNT cloning.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000178691 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000017548 - 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. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (August 1995). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 2 (4): 167–74, 199–210. doi: 10.1093/dnares/2.4.167 . PMID   8590280.
  6. Koontz JI, Soreng AL, Nucci M, Kuo FC, Pauwels P, van Den Berghe H, Dal Cin P, Fletcher JA, Sklar J (May 2001). "Frequent fusion of the JAZF1 and JJAZ1 genes in endometrial stromal tumors". Proceedings of the National Academy of Sciences of the United States of America. 98 (11): 6348–53. Bibcode:2001PNAS...98.6348K. doi: 10.1073/pnas.101132598 . PMC   33471 . PMID   11371647.
  7. Ross PJ, Ragina NP, Rodriguez RM, Iager AE, Siripattarapravat K, Lopez-Corrales N, Cibelli JB (December 2008). "Polycomb gene expression and histone H3 lysine 27 trimethylation changes during bovine preimplantation development". Reproduction. 136 (6): 777–85. doi: 10.1530/REP-08-0045 . PMID   18784248.
  8. 1 2 "Entrez Gene: SUZ12 suppressor of zeste 12 homolog (Drosophila)".
  9. Rinn JL, Kertesz M, Wang JK, Squazzo SL, Xu X, Brugmann SA, Goodnough LH, Helms JA, Farnham PJ, Segal E, Chang HY (June 2007). "Functional demarcation of active and silent chromatin domains in human HOX loci by noncoding RNAs". Cell. 129 (7): 1311–23. doi:10.1016/j.cell.2007.05.022. PMC   2084369 . PMID   17604720.

Further reading