SUPT16H: Difference between revisions

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Latest revision as of 07:18, 11 September 2017

FACT complex subunit SPT16 is a protein that in humans is encoded by the SUPT16H gene.^[1]^[2]^[3]

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.^[3]

Interactions

SUPT16H has been shown to interact with BAZ1B.^[4]

References

↑ 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.
↑ 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.
↑ ^3.0 ^3.1 "Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)".
↑ Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (Jun 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID 12837248.

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. 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. doi:10.1046/j.1365-2443.2000.00323.x. PMID 10792464.
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.
Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID 12837248.
Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D (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, 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.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[pmid9489704-1] 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.

[pmid11239457-2] 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.

[entrez-3] 3.0 ^3.1 "Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)".

[pmid12837248-4] Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (Jun 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID 12837248.

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''FACT complex subunit SPT16''' is a [[protein]] that in humans is encoded by the ''SUPT16H'' [[gene]].<ref name="pmid9489704">{{cite journal | vauthors = Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D | title = FACT, a factor that facilitates transcript elongation through nucleosomes | journal = Cell | volume = 92 | issue = 1 | pages = 105–16 | date = Mar 1998 | pmid = 9489704 | pmc =  | doi = 10.1016/S0092-8674(00)80903-4 }}</ref><ref name="pmid11239457">{{cite journal | vauthors = Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H | title = A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1 | journal = Mol Cell | volume = 7 | issue = 2 | pages = 283–92 | date = Mar 2001 | pmid = 11239457 | pmc =  | doi = 10.1016/S1097-2765(01)00176-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198| accessdate = }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Suppressor of Ty 16 homolog (S. cerevisiae)
- | HGNCid = 11465
- | Symbol = SUPT16H
- | AltSymbols =; FACT; CDC68; FACTP140; FLJ10857; FLJ14010; FLJ34357; SPT16/CDC68
- | OMIM = 605012
- | ECnumber =
- | Homologene = 5207
- | MGIid = 1890948
- | GeneAtlas_image1 = PBB_GE_SUPT16H_217815_at_tn.png
- | Function = {{GNF_GO|id=GO:0008159 |text = positive transcription elongation factor activity}} {{GNF_GO|id=GO:0008235 |text = metalloexopeptidase activity}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
- | Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006337 |text = nucleosome disassembly}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006508 |text = proteolysis}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 11198
-    | Hs_Ensembl = ENSG00000092201
-    | Hs_RefseqProtein = NP_009123
-    | Hs_RefseqmRNA = NM_007192
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 14
-    | Hs_GenLoc_start = 20889478
-    | Hs_GenLoc_end = 20922265
-    | Hs_Uniprot = Q9Y5B9
-    | Mm_EntrezGene = 114741
-    | Mm_Ensembl = ENSMUSG00000035726
-    | Mm_RefseqmRNA = NM_033618
-    | Mm_RefseqProtein = NP_291096
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 14
-    | Mm_GenLoc_start = 51082365
-    | Mm_GenLoc_end = 51119152
-    | Mm_Uniprot = Q920B9
-  }}
-}}
-'''Suppressor of Ty 16 homolog (S. cerevisiae)''', also known as '''SUPT16H''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+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 (biology)|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.<ref name="entrez" />
-{{PBB_Summary
-| section_title =
-| summary_text = 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_(biology)|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.<ref name="entrez">{{cite web | title = Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198| accessdate = }}</ref>
-}}
-==References==
+== Interactions ==
-{{reflist|2}}
-==Further reading==
+SUPT16H has been shown to [[Protein-protein interaction|interact]] with [[BAZ1B]].<ref name=pmid12837248>{{cite journal | vauthors = Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S | title = The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome | journal = Cell | volume = 113 | issue = 7 | pages = 905–17 | date = Jun 2003 | pmid = 12837248 | doi = 10.1016/S0092-8674(03)00436-7 }}</ref>
+== References ==
+{{reflist}}
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+* {{cite journal | vauthors = LeRoy G, Orphanides G, Lane WS, Reinberg D | title = Requirement of RSF and FACT for transcription of chromatin templates in vitro | journal = Science | volume = 282 | issue = 5395 | pages = 1900–4 | year = 1998 | pmid = 9836642 | doi = 10.1126/science.282.5395.1900 }}
-| citations =
+* {{cite journal | vauthors = Orphanides G, Wu WH, Lane WS, Hampsey M, Reinberg D | title = The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins | journal = Nature | volume = 400 | issue = 6741 | pages = 284–8 | year = 1999 | pmid = 10421373 | doi = 10.1038/22350 }}
-*{{cite journal  | author=Orphanides G, LeRoy G, Chang CH, ''et al.'' |title=FACT, a factor that facilitates transcript elongation through nucleosomes. |journal=Cell |volume=92 |issue= 1 |pages= 105-16 |year= 1998 |pmid= 9489704 |doi=  }}
+* {{cite journal | vauthors = Kang SW, Kuzuhara T, Horikoshi M | title = Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68 | journal = Genes Cells | volume = 5 | issue = 4 | pages = 251–63 | year = 2000 | pmid = 10792464 | doi = 10.1046/j.1365-2443.2000.00323.x }}
-*{{cite journal  | author=LeRoy G, Orphanides G, Lane WS, Reinberg D |title=Requirement of RSF and FACT for transcription of chromatin templates in vitro. |journal=Science |volume=282 |issue= 5395 |pages= 1900-4 |year= 1998 |pmid= 9836642 |doi=  }}
+* {{cite journal | vauthors = Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H | title = FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH | journal = Mol. Cell | volume = 5 | issue = 6 | pages = 1067–72 | year = 2000 | pmid = 10912001 | doi = 10.1016/S1097-2765(00)80272-5 }}
-*{{cite journal  | author=Orphanides G, Wu WH, Lane WS, ''et al.'' |title=The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. |journal=Nature |volume=400 |issue= 6741 |pages= 284-8 |year= 1999 |pmid= 10421373 |doi= 10.1038/22350 }}
+* {{cite journal | vauthors = Keller DM, Lu H | title = p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex | journal = J. Biol. Chem. | volume = 277 | issue = 51 | pages = 50206–13 | year = 2003 | pmid = 12393879 | doi = 10.1074/jbc.M209820200 }}
-*{{cite journal  | author=Kang SW, Kuzuhara T, Horikoshi M |title=Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68. |journal=Genes Cells |volume=5 |issue= 4 |pages= 251-63 |year= 2000 |pmid= 10792464 |doi=  }}
+* {{cite journal | vauthors = Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S | title = The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome | journal = Cell | volume = 113 | issue = 7 | pages = 905–17 | year = 2003 | pmid = 12837248 | doi = 10.1016/S0092-8674(03)00436-7 }}
-*{{cite journal  | author=Wada T, Orphanides G, Hasegawa J, ''et al.'' |title=FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH. |journal=Mol. Cell |volume=5 |issue= 6 |pages= 1067-72 |year= 2000 |pmid= 10912001 |doi=  }}
+* {{cite journal | vauthors = Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D | title = FACT facilitates transcription-dependent nucleosome alteration | journal = Science | volume = 301 | issue = 5636 | pages = 1090–3 | year = 2003 | pmid = 12934006 | doi = 10.1126/science.1085703 }}
-*{{cite journal  | author=Keller DM, Zeng X, Wang Y, ''et al.'' |title=A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. |journal=Mol. Cell |volume=7 |issue= 2 |pages= 283-92 |year= 2001 |pmid= 11239457 |doi=  }}
+* {{cite journal | vauthors = Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG | title = Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins | journal = Mol. Cell. Biol. | volume = 23 | issue = 21 | pages = 7437–47 | year = 2003 | pmid = 14559993 | pmc = 207616 | doi = 10.1128/MCB.23.21.7437-7447.2003 }}
-*{{cite journal  | author=Keller DM, Lu H |title=p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50206-13 |year= 2003 |pmid= 12393879 |doi= 10.1074/jbc.M209820200 }}
+* {{cite journal | vauthors = Tan BC, Lee SC | title = Nek9, a novel FACT-associated protein, modulates interphase progression | journal = J. Biol. Chem. | volume = 279 | issue = 10 | pages = 9321–30 | year = 2004 | pmid = 14660563 | doi = 10.1074/jbc.M311477200 }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+* {{cite journal | vauthors = Fryer CJ, White JB, Jones KA | title = Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover | journal = Mol. Cell | volume = 16 | issue = 4 | pages = 509–20 | year = 2005 | pmid = 15546612 | doi = 10.1016/j.molcel.2004.10.014 }}
-*{{cite journal  | author=Kitagawa H, Fujiki R, Yoshimura K, ''et al.'' |title=The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome. |journal=Cell |volume=113 |issue= 7 |pages= 905-17 |year= 2003 |pmid= 12837248 |doi=  }}
+* {{cite journal | vauthors = Kouskouti A, Talianidis I | title = Histone modifications defining active genes persist after transcriptional and mitotic inactivation | journal = EMBO J. | volume = 24 | issue = 2 | pages = 347–57 | year = 2005 | pmid = 15616580 | pmc = 545808 | doi = 10.1038/sj.emboj.7600516 }}
-*{{cite journal  | author=Belotserkovskaya R, Oh S, Bondarenko VA, ''et al.'' |title=FACT facilitates transcription-dependent nucleosome alteration. |journal=Science |volume=301 |issue= 5636 |pages= 1090-3 |year= 2003 |pmid= 12934006 |doi= 10.1126/science.1085703 }}
+* {{cite journal | vauthors = Huang JY, Chen WH, Chang YL, Wang HT, Chuang WT, Lee SC | title = Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation | journal = Nucleic Acids Res. | volume = 34 | issue = 8 | pages = 2398–407 | year = 2006 | pmid = 16682447 | pmc = 1458519 | doi = 10.1093/nar/gkl241 }}
-*{{cite journal  | author=Li J, Hawkins IC, Harvey CD, ''et al.'' |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437-47 |year= 2003 |pmid= 14559993 |doi=  }}
+* {{cite journal | vauthors = Pavri R, Zhu B, Li G, Trojer P, Mandal S, Shilatifard A, Reinberg D | title = Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II | journal = Cell | volume = 125 | issue = 4 | pages = 703–17 | year = 2006 | pmid = 16713563 | doi = 10.1016/j.cell.2006.04.029 }}
-*{{cite journal  | author=Tan BC, Lee SC |title=Nek9, a novel FACT-associated protein, modulates interphase progression. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 9321-30 |year= 2004 |pmid= 14660563 |doi= 10.1074/jbc.M311477200 }}
+* {{cite journal | vauthors = Tan BC, Chien CT, Hirose S, Lee SC | title = Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication | journal = EMBO J. | volume = 25 | issue = 17 | pages = 3975–85 | year = 2006 | pmid = 16902406 | pmc = 1560368 | doi = 10.1038/sj.emboj.7601271 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+* {{cite journal | vauthors = Biswas D, Dutta-Biswas R, Mitra D, Shibata Y, Strahl BD, Formosa T, Stillman DJ | title = Opposing roles for Set2 and yFACT in regulating TBP binding at promoters | journal = EMBO J. | volume = 25 | issue = 19 | pages = 4479–89 | year = 2006 | pmid = 16977311 | pmc = 1589996 | doi = 10.1038/sj.emboj.7601333 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
-*{{cite journal  | author=Fryer CJ, White JB, Jones KA |title=Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover. |journal=Mol. Cell |volume=16 |issue= 4 |pages= 509-20 |year= 2005 |pmid= 15546612 |doi= 10.1016/j.molcel.2004.10.014 }}
-*{{cite journal  | author=Kouskouti A, Talianidis I |title=Histone modifications defining active genes persist after transcriptional and mitotic inactivation. |journal=EMBO J. |volume=24 |issue= 2 |pages= 347-57 |year= 2005 |pmid= 15616580 |doi= 10.1038/sj.emboj.7600516 }}
-*{{cite journal  | author=Huang JY, Chen WH, Chang YL, ''et al.'' |title=Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation. |journal=Nucleic Acids Res. |volume=34 |issue= 8 |pages= 2398-407 |year= 2006 |pmid= 16682447 |doi= 10.1093/nar/gkl241 }}
-*{{cite journal  | author=Pavri R, Zhu B, Li G, ''et al.'' |title=Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. |journal=Cell |volume=125 |issue= 4 |pages= 703-17 |year= 2006 |pmid= 16713563 |doi= 10.1016/j.cell.2006.04.029 }}
-*{{cite journal  | author=Tan BC, Chien CT, Hirose S, Lee SC |title=Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication. |journal=EMBO J. |volume=25 |issue= 17 |pages= 3975-85 |year= 2006 |pmid= 16902406 |doi= 10.1038/sj.emboj.7601271 }}
-*{{cite journal  | author=Biswas D, Dutta-Biswas R, Mitra D, ''et al.'' |title=Opposing roles for Set2 and yFACT in regulating TBP binding at promoters. |journal=EMBO J. |volume=25 |issue= 19 |pages= 4479-89 |year= 2006 |pmid= 16977311 |doi= 10.1038/sj.emboj.7601333 }}
-}}
 {{refend}}
-{{protein-stub}}
-{{WikiDoc Sources}}
+{{gene-14-stub}}

SUPT16H: Difference between revisions

Latest revision as of 07:18, 11 September 2017

Contents

Function

Interactions

References

Further reading

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