SUPT5H

SUPT5H
Available structures
PDB	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	OMIM: 602102; MGI: 1202400; HomoloGene: 2384; GeneCards: SUPT5H; OMA:SUPT5H - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	39,476,670 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	28,038,171 bp
RNA expression pattern
	Top expressed in
	right testis; ; left testis; ; anterior pituitary; ; sural nerve; ; right hemisphere of cerebellum; ; right lobe of thyroid gland; ; right uterine tube; ; left lobe of thyroid gland; ; apex of heart; ; right frontal lobe;
	Top expressed in
	adrenal gland; ; Gonadal ridge; ; internal carotid artery; ; external carotid artery; ; fossa; ; crypt of lieberkuhn of small intestine; ; lacrimal gland; ; tail of embryo; ; vestibular membrane of cochlear duct; ; motor neuron;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding; protein heterodimerization activity; enzyme binding; chromatin binding; RNA binding; DNA binding; mRNA binding;
Cellular component	nucleoplasm; DSIF complex; nucleus;
Biological process	chromatin remodeling; negative regulation of mRNA polyadenylation; regulation of transcription, DNA-templated; regulation of transcription by RNA polymerase II; transcription elongation from RNA polymerase II promoter; regulation of DNA-templated transcription, elongation; negative regulation of transcription by RNA polymerase II; 7-methylguanosine mRNA capping; transcription by RNA polymerase II; 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 by RNA polymerase II;
	Sources:Amigo / QuickGO
Orthologs
	6829
	20924
	ENSG00000196235
	ENSMUSG00000003435
	O00267
	O55201
NM_001111020; NM_001130824; NM_001130825; NM_003169; NM_001319990;
	NM_001319991
	NM_013676
NP_001104490; NP_001124296; NP_001124297; NP_001306919; NP_001306920;
	NP_003160
	NP_038704
	Wikidata
View/Edit Human	View/Edit Mouse

Transcription elongation factor SPT5 is a protein that in humans is encoded by the SUPT5H gene.^[5]^[6]

Interactions

SUPT5H has been shown to interact with:

CDK9,^[7]
Cyclin-dependent kinase 7,^[7]
HTATSF1,^[8]
PIN1,^[9]
POLR2A,^[8]^[10]
PRMT1^[11] and
Protein arginine methyltransferase 5.^[11]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000196235 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003435 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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)".
^ ^a ^b 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.
^ ^a ^b 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.
^ ^a ^b 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.

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. S2CID 43730950.
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. S2CID 16855257.
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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000196235 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003435 – 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.

[pmid8975720-5] 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.

[6] "Entrez Gene: SUPT5H Suppressor of Ty 5 homolog (S. cerevisiae)".

[pmid10958691-7] 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.

[pmid10454543-8] 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.

[pmid11575923-9] 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.

[pmid9450929-10] 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.

[pmid12718890-11] 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.

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Interactions

References

Further reading