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SUPT5H

Introduction

Transcription elongation factor SPT5 is a protein that in humans is encoded by the SUPT5H gene.[1][2]

Interactions

Interactions

SUPT5H has been shown to interact with:

Model organisms

Model organisms

Model organisms have been used in the study of SUPT5H function. A conditional knockout mouse line called Supt5tm2a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: – In-depth immunological phenotyping[14]

References

References

  1. ↑ Chiang PW, Fogel E, Jackson CL, Lieuallen K, Lennon G, Qu X, Wang SQ, Kurnit DM (Dec 1996). “Isolation, sequencing, and mapping of the human homologue of the yeast transcription factor, SPT5”. Genomics. 38 (3): 421–4. doi:10.1006/geno.1996.0646. PMIDΒ 8975720.
  2. ↑ “Entrez Gene: SUPT5H Suppressor of Ty 5 homolog (S. cerevisiae)”.
  3. ↑ 3.0 3.1 Garber ME, Mayall TP, Suess EM, Meisenhelder J, Thompson NE, Jones KA (Sep 2000). “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. doi:10.1128/mcb.20.18.6958-6969.2000. PMCΒ 88771. PMIDΒ 10958691.
  4. ↑ 4.0 4.1 Kim JB, Yamaguchi Y, Wada T, Handa H, Sharp PA (Sep 1999). “Tat-SF1 protein associates with RAP30 and human SPT5 proteins”. Molecular and Cellular Biology. 19 (9): 5960–8. doi:10.1128/mcb.19.9.5960. PMCΒ 84462. PMIDΒ 10454543.
  5. ↑ Lavoie SB, Albert AL, Handa H, Vincent M, Bensaude O (Sep 2001). “The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9”. Journal of Molecular Biology. 312 (4): 675–85. doi:10.1006/jmbi.2001.4991. PMIDΒ 11575923.
  6. ↑ Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H (Feb 1998). “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. doi:10.1101/gad.12.3.343. PMCΒ 316480. PMIDΒ 9450929.
  7. ↑ 7.0 7.1 Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB (Apr 2003). “Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties”. Molecular Cell. 11 (4): 1055–66. doi:10.1016/s1097-2765(03)00101-1. PMIDΒ 12718890.
  8. ↑ Gerdin AK (2010). “The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice”. Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  9. ↑ 9.0 9.1 “International Mouse Phenotyping Consortium”.
  10. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). “A conditional knockout resource for the genome-wide study of mouse gene function”. Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMCΒ 3572410. PMIDΒ 21677750.
  11. ↑ Dolgin E (Jun 2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMIDΒ 21677718.
  12. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). “A mouse for all reasons”. Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMIDΒ 17218247.
  13. ↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). “Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes”. Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMCΒ 3717207. PMIDΒ 23870131.
  14. ↑ 14.0 14.1 “Infection and Immunity Immunophenotyping (3i) Consortium”.
Further reading

Further reading