Biology:SUPT5H
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Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
Transcription elongation factor SPT5 is a protein that in humans is encoded by the SUPT5H gene.[1][2] Together with hSPT4, it composes DSIF in humans.[3]
Interactions
SUPT5H has been shown to interact with:
References
- ↑ "Isolation, sequencing, and mapping of the human homologue of the yeast transcription factor, SPT5". Genomics 38 (3): 421–4. Dec 1996. doi:10.1006/geno.1996.0646. PMID 8975720.
- ↑ "Entrez Gene: SUPT5H Suppressor of Ty 5 homolog (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6829.
- ↑ "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes & Development 12 (3): 343–356. February 1998. doi:10.1101/gad.12.3.343. PMID 9450929.
- ↑ 4.0 4.1 "CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA". Molecular and Cellular Biology 20 (18): 6958–69. Sep 2000. doi:10.1128/mcb.20.18.6958-6969.2000. PMID 10958691.
- ↑ 5.0 5.1 "Tat-SF1 protein associates with RAP30 and human SPT5 proteins". Molecular and Cellular Biology 19 (9): 5960–8. Sep 1999. doi:10.1128/mcb.19.9.5960. PMID 10454543.
- ↑ "The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9". Journal of Molecular Biology 312 (4): 675–85. Sep 2001. doi:10.1006/jmbi.2001.4991. PMID 11575923.
- ↑ "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes & Development 12 (3): 343–56. Feb 1998. doi:10.1101/gad.12.3.343. PMID 9450929.
- ↑ 8.0 8.1 "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Molecular Cell 11 (4): 1055–66. Apr 2003. doi:10.1016/s1097-2765(03)00101-1. PMID 12718890.
Further reading
- "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry 236 (1): 107–13. Apr 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Large-scale concatenation cDNA sequencing". Genome Research 7 (4): 353–8. Apr 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis". FEBS Letters 409 (1): 74–8. Jun 1997. doi:10.1016/S0014-5793(97)00486-9. PMID 9199507. Bibcode: 1997FEBSL.409...74S.
- "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes & Development 12 (3): 343–56. Feb 1998. doi:10.1101/gad.12.3.343. PMID 9450929.
- "Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation". Journal of Molecular Biology 277 (2): 179–97. Mar 1998. doi:10.1006/jmbi.1997.1601. PMID 9514752.
- "Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro". The EMBO Journal 17 (24): 7395–403. Dec 1998. doi:10.1093/emboj/17.24.7395. PMID 9857195.
- "Structure and function of the human transcription elongation factor DSIF". The Journal of Biological Chemistry 274 (12): 8085–92. Mar 1999. doi:10.1074/jbc.274.12.8085. PMID 10075709.
- "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation". Cell 97 (1): 41–51. Apr 1999. doi:10.1016/S0092-8674(00)80713-8. PMID 10199401.
- "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription". The EMBO Journal 18 (13): 3688–701. Jul 1999. doi:10.1093/emboj/18.13.3688. PMID 10393184.
- "Transcription elongation factor hSPT5 stimulates mRNA capping". Genes & Development 13 (14): 1774–9. Jul 1999. doi:10.1101/gad.13.14.1774. PMID 10421630.
- "Tat-SF1 protein associates with RAP30 and human SPT5 proteins". Molecular and Cellular Biology 19 (9): 5960–8. Sep 1999. doi:10.1128/mcb.19.9.5960. PMID 10454543.
- "Domains in the SPT5 protein that modulate its transcriptional regulatory properties". Molecular and Cellular Biology 20 (9): 2970–83. May 2000. doi:10.1128/MCB.20.9.2970-2983.2000. PMID 10757782.
- "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH". Molecular Cell 5 (6): 1067–72. Jun 2000. doi:10.1016/S1097-2765(00)80272-5. PMID 10912001.
- "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation". The Journal of Biological Chemistry 276 (16): 12951–8. Apr 2001. doi:10.1074/jbc.M006130200. PMID 11112772.
- "Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase". The Journal of Biological Chemistry 276 (15): 12317–23. Apr 2001. doi:10.1074/jbc.M010908200. PMID 11145967.
- "A highly purified RNA polymerase II elongation control system". The Journal of Biological Chemistry 276 (45): 42601–9. Nov 2001. doi:10.1074/jbc.M104967200. PMID 11553615.
- "The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9". Journal of Molecular Biology 312 (4): 675–85. Sep 2001. doi:10.1006/jmbi.2001.4991. PMID 11575923.
- "Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences". Molecular and Cellular Biology 22 (4): 1079–93. Feb 2002. doi:10.1128/MCB.22.4.1079-1093.2002. PMID 11809800.
- "Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA". Molecular and Cellular Biology 22 (9): 2918–27. May 2002. doi:10.1128/MCB.22.9.2918-2927.2002. PMID 11940650.
