SUPT16H

From Wikipedia, the free encyclopedia

Suppressor of Ty 16 homolog (S. cerevisiae)

Identifiers

SUPT16H; FACT; CDC68; FACTP140; FLJ10857; FLJ14010; FLJ34357; SPT16/CDC68

External IDs

OMIM: 605012 MGI: 1890948 HomoloGene: 5207

Gene ontology
Molecular Function:	• positive transcription elongation factor activity • metalloexopeptidase activity
Cellular Component:	• nucleus • chromosome
Biological Process:	• DNA replication • DNA repair • nucleosome disassembly • transcription • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_007192 (mRNA)
NP_009123 (protein)

NM_033618 (mRNA)
NP_291096 (protein)

Location

Chr 14: 20.89 - 20.92 Mb

Chr 14: 51.08 - 51.12 Mb

Pubmed search

[1]

[2]

Suppressor of Ty 16 homolog (S. cerevisiae), also known as SUPT16H, is a human gene.^[1]

Transcription of protein-coding genes can be reconstituted on naked DNA with only the general transcription factors and RNA polymerase II. However, this minimal system cannot transcribe DNA packaged into chromatin, indicating that accessory factors may facilitate access to DNA. One such factor, FACT (facilitates chromatin transcription), interacts specifically with histones H2A/H2B to effect nucleosome disassembly and transcription elongation. FACT is composed of an 80 kDa subunit and a 140 kDa subunit, the latter of which is the protein encoded by this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae).

[edit] Further reading

Orphanides G, LeRoy G, Chang CH, et al. (1998). "FACT, a factor that facilitates transcript elongation through nucleosomes.". Cell 92 (1): 105–16. PMID 9489704.
LeRoy G, Orphanides G, Lane WS, Reinberg D (1998). "Requirement of RSF and FACT for transcription of chromatin templates in vitro.". Science 282 (5395): 1900–4. PMID 9836642.
Orphanides G, Wu WH, Lane WS, et al. (1999). "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.". Nature 400 (6741): 284–8. doi:10.1038/22350. PMID 10421373.
Kang SW, Kuzuhara T, Horikoshi M (2000). "Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68.". Genes Cells 5 (4): 251–63. PMID 10792464.
Wada T, Orphanides G, Hasegawa J, et al. (2000). "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH.". Mol. Cell 5 (6): 1067–72. PMID 10912001.
Keller DM, Zeng X, Wang Y, et al. (2001). "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.". Mol. Cell 7 (2): 283–92. PMID 11239457.
Keller DM, Lu H (2003). "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex.". J. Biol. Chem. 277 (51): 50206–13. doi:10.1074/jbc.M209820200. PMID 12393879.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Kitagawa H, Fujiki R, Yoshimura K, et al. (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome.". Cell 113 (7): 905–17. PMID 12837248.
Belotserkovskaya R, Oh S, Bondarenko VA, et al. (2003). "FACT facilitates transcription-dependent nucleosome alteration.". Science 301 (5636): 1090–3. doi:10.1126/science.1085703. PMID 12934006.
Li J, Hawkins IC, Harvey CD, et al. (2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins.". Mol. Cell. Biol. 23 (21): 7437–47. PMID 14559993.
Tan BC, Lee SC (2004). "Nek9, a novel FACT-associated protein, modulates interphase progression.". J. Biol. Chem. 279 (10): 9321–30. doi:10.1074/jbc.M311477200. PMID 14660563.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Fryer CJ, White JB, Jones KA (2005). "Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover.". Mol. Cell 16 (4): 509–20. doi:10.1016/j.molcel.2004.10.014. PMID 15546612.
Kouskouti A, Talianidis I (2005). "Histone modifications defining active genes persist after transcriptional and mitotic inactivation.". EMBO J. 24 (2): 347–57. doi:10.1038/sj.emboj.7600516. PMID 15616580.
Huang JY, Chen WH, Chang YL, et al. (2006). "Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation.". Nucleic Acids Res. 34 (8): 2398–407. doi:10.1093/nar/gkl241. PMID 16682447.
Pavri R, Zhu B, Li G, et al. (2006). "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.". Cell 125 (4): 703–17. doi:10.1016/j.cell.2006.04.029. PMID 16713563.
Tan BC, Chien CT, Hirose S, Lee SC (2006). "Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication.". EMBO J. 25 (17): 3975–85. doi:10.1038/sj.emboj.7601271. PMID 16902406.
Biswas D, Dutta-Biswas R, Mitra D, et al. (2006). "Opposing roles for Set2 and yFACT in regulating TBP binding at promoters.". EMBO J. 25 (19): 4479–89. doi:10.1038/sj.emboj.7601333. PMID 16977311.