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SUPT16H
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5E5B, 4Z2M, 4Z2N
Identifiers
Aliases	SUPT16H, CDC68, FACTP140, SPT16/CDC68, SPT16, SPT16 homolog, facilitates chromatin remodeling subunit, NEDDFAC
External IDs	OMIM: 605012; MGI: 1890948; HomoloGene: 5207; GeneCards: SUPT16H; OMA:SUPT16H - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q11.2 Start 21,351,476 bp End 21,384,019 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14 C2|14 26.83 cM Start 52,397,871 bp End 52,434,873 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence gonad testicle Achilles tendon epithelium of colon cerebellar hemisphere right hemisphere of cerebellum body of uterus smooth muscle tissue Top expressed in fetal liver hematopoietic progenitor cell genital tubercle tail of embryo neural layer of retina primitive streak renal corpuscle epiblast tibiofemoral joint medullary collecting duct pineal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding nucleosome binding histone binding RNA binding Cellular component nucleus nucleoplasm chromosome FACT complex Biological process positive regulation of DNA-templated transcription, elongation DNA replication nucleosome disassembly regulation of transcription, DNA-templated transcription by RNA polymerase II DNA repair transcription, DNA-templated cellular response to DNA damage stimulus regulation of signal transduction by p53 class mediator transcription elongation from RNA polymerase II promoter positive regulation of transcription elongation from RNA polymerase II promoter Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11198 114741 Ensembl ENSG00000092201 ENSMUSG00000035726 UniProt Q9Y5B9 Q920B9 RefSeq (mRNA) NM_007192 NM_033618 RefSeq (protein) NP_009123 NP_291096 Location (UCSC) Chr 14: 21.35 – 21.38 Mb Chr 14: 52.4 – 52.43 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

FACT complex subunit SPT16 is a protein that in humans is encoded by the SUPT16H gene.

Function

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000092201 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000035726 – 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. Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D (Mar 1998). "FACT, a factor that facilitates transcript elongation through nucleosomes". Cell. 92 (1): 105–16. doi:10.1016/S0092-8674(00)80903-4. PMID 9489704.
6. Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H (Mar 2001). "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1". Mol Cell. 7 (2): 283–92. doi:10.1016/S1097-2765(01)00176-9. PMID 11239457.
7. ^ "Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)".

Further reading

• 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. doi:10.1126/science.282.5395.1900. PMID 9836642.
• Orphanides G, Wu WH, Lane WS, Hampsey M, Reinberg D (1999). "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins". Nature. 400 (6741): 284–8. Bibcode:1999Natur.400..284O. doi:10.1038/22350. PMID 10421373. S2CID 4300397.
• 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. doi:10.1046/j.1365-2443.2000.00323.x. PMID 10792464. S2CID 33454256.
• Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H (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. doi:10.1016/S1097-2765(00)80272-5. PMID 10912001.
• 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.
• Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D (2003). "FACT facilitates transcription-dependent nucleosome alteration". Science. 301 (5636): 1090–3. Bibcode:2003Sci...301.1090B. doi:10.1126/science.1085703. PMID 12934006. S2CID 26667338.
• Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (2003). "Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. 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.
• 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. PMC 545808. PMID 15616580.
• Huang JY, Chen WH, Chang YL, Wang HT, Chuang WT, Lee SC (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. PMC 1458519. PMID 16682447.
• Pavri R, Zhu B, Li G, Trojer P, Mandal S, Shilatifard A, Reinberg D (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. PMC 1560368. PMID 16902406.
• Biswas D, Dutta-Biswas R, Mitra D, Shibata Y, Strahl BD, Formosa T, Stillman DJ (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. PMC 1589996. PMID 16977311.

External links

• Overview of all the structural information available in the PDB for UniProt: Q9Y5B9 (FACT complex subunit SPT16) at the PDBe-KB.

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