SUPT5H

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2DO3, 2E6Z, 2E70, 3H7H, 4L1U

Identifiers

Aliases

SUPT5H, SPT5, SPT5H, Tat-CT1, SPT5 homolog, DSIF elongation factor subunit

External IDs

MGI: 1202400 HomoloGene: 2384 GeneCards: SUPT5H

Gene ontology
Molecular function	• protein binding • protein heterodimerization activity • enzyme binding • poly(A) RNA binding • chromatin binding
Cellular component	• nucleoplasm • DSIF complex • nucleus
Biological process	• chromatin remodeling • negative regulation of mRNA polyadenylation • regulation of transcription, DNA-templated • regulation of transcription from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • regulation of DNA-templated transcription, elongation • negative regulation of transcription from RNA polymerase II promoter • 7-methylguanosine mRNA capping • transcription from RNA polymerase II promoter • response to organic substance • transcription, DNA-templated • negative regulation of DNA-templated transcription, elongation • positive regulation of DNA-templated transcription, elongation • positive regulation of macroautophagy • DNA-templated transcription, elongation • single stranded viral RNA replication via double stranded DNA intermediate • positive regulation of viral transcription • cell cycle • positive regulation of transcription from RNA polymerase II promoter
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


6829


20924

Ensembl


ENSG00000196235


ENSMUSG00000003435

UniProt


O00267


O55201

RefSeq (mRNA)

NM_001111020 NM_001130824 NM_001130825 NM_003169 NM_001319990
NM_001319991


NM_013676

RefSeq (protein)

NP_001104490.1 NP_001124296.1 NP_001124297.1 NP_003160.2 NP_001306919.1
NP_001306920.1


NP_038704.1

Location (UCSC)

Chr 19: 39.44 – 39.48 Mb

Chr 7: 28.31 – 28.34 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Transcription elongation factor SPT5 is a protein that in humans is encoded by the SUPT5H gene.^[3]^[4]

Interactions

SUPT5H has been shown to interact with:

CDK9,^[5]
Cyclin-dependent kinase 7,^[5]
HTATSF1,^[6]
PIN1,^[7]
POLR2A,^[6]^[8]
PRMT1^[9] and
Protein arginine methyltransferase 5.^[9]

Model organisms

Model organisms have been used in the study of SUPT5H function. A conditional knockout mouse line called Supt5^{tm2a(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[10] Male and female animals underwent a standardized phenotypic screen^[11] to determine the effects of deletion.^[12]^[13]^[14]^[15] Additional screens performed: - In-depth immunological phenotyping^[16]

*Supt5* knockout mouse phenotype
Characteristic	Phenotype
All data available at.^[11]^[16]
Peripheral blood leukocytes 6 Weeks	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 8975720.
↑ "Entrez Gene: SUPT5H Suppressor of Ty 5 homolog (S. cerevisiae)".
1 2 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. PMC 88771. PMID 10958691.
1 2 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. PMC 84462. PMID 10454543.
↑ 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. PMID 11575923.
↑ 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. PMC 316480. PMID 9450929.
1 2 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. PMID 12718890.
↑ 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.
1 2 "International Mouse Phenotyping Consortium".
↑ 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. PMC 3572410. PMID 21677750.
↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ 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. PMID 17218247.
↑ 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. PMC 3717207. PMID 23870131.
1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".

Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Stachora AA, Schäfer RE, Pohlmeier M, Maier G, Ponstingl H (Jun 1997). "Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis". FEBS Letters. 409 (1): 74–8. doi:10.1016/S0014-5793(97)00486-9. PMID 9199507.
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. PMC 316480. PMID 9450929.
Wu-Baer F, Lane WS, Gaynor RB (Mar 1998). "Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation". Journal of Molecular Biology. 277 (2): 179–97. doi:10.1006/jmbi.1997.1601. PMID 9514752.
Wada T, Takagi T, Yamaguchi Y, Watanabe D, Handa H (Dec 1998). "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. doi:10.1093/emboj/17.24.7395. PMC 1171084. PMID 9857195.
Yamaguchi Y, Wada T, Watanabe D, Takagi T, Hasegawa J, Handa H (Mar 1999). "Structure and function of the human transcription elongation factor DSIF". The Journal of Biological Chemistry. 274 (12): 8085–92. doi:10.1074/jbc.274.12.8085. PMID 10075709.
Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H (Apr 1999). "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation". Cell. 97 (1): 41–51. doi:10.1016/S0092-8674(00)80713-8. PMID 10199401.
Parada CA, Roeder RG (Jul 1999). "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription". The EMBO Journal. 18 (13): 3688–701. doi:10.1093/emboj/18.13.3688. PMC 1171446. PMID 10393184.
Wen Y, Shatkin AJ (Jul 1999). "Transcription elongation factor hSPT5 stimulates mRNA capping". Genes & Development. 13 (14): 1774–9. doi:10.1101/gad.13.14.1774. PMC 316881. PMID 10421630.
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. PMC 84462. PMID 10454543.
Ivanov D, Kwak YT, Guo J, Gaynor RB (May 2000). "Domains in the SPT5 protein that modulate its transcriptional regulatory properties". Molecular and Cellular Biology. 20 (9): 2970–83. doi:10.1128/MCB.20.9.2970-2983.2000. PMC 85557. PMID 10757782.
Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H (Jun 2000). "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH". Molecular Cell. 5 (6): 1067–72. doi:10.1016/S1097-2765(00)80272-5. PMID 10912001.
Ping YH, Rana TM (Apr 2001). "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. doi:10.1074/jbc.M006130200. PMID 11112772.
Kim JB, Sharp PA (Apr 2001). "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. doi:10.1074/jbc.M010908200. PMID 11145967.
Renner DB, Yamaguchi Y, Wada T, Handa H, Price DH (Nov 2001). "A highly purified RNA polymerase II elongation control system". The Journal of Biological Chemistry. 276 (45): 42601–9. doi:10.1074/jbc.M104967200. PMID 11553615.
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. PMID 11575923.
Bourgeois CF, Kim YK, Churcher MJ, West MJ, Karn J (Feb 2002). "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. doi:10.1128/MCB.22.4.1079-1093.2002. PMC 134635. PMID 11809800.
Yamaguchi Y, Inukai N, Narita T, Wada T, Handa H (May 2002). "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. doi:10.1128/MCB.22.9.2918-2927.2002. PMC 133766. PMID 11940650.

PDB gallery

2do3: Solution structure of the third KOW motif of transcription elongation factor SPT5

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SUPT5H

Interactions

Model organisms

References

Further reading