YEAST:TFS2

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	DST1 (synonyms: PPR2)
Protein Name(s)	Transcription elongation factor S-II DNA strand transfer protein alpha STP-alpha DNA strand transferase 1 Pyrimidine pathway regulatory protein 2
External Links
UniProt	P07273
EMBL	M36724 D12478 M60770 Z72565 X00047 BK006941
PIR	A42921
RefSeq	NP_011472.1
PDB	1ENW 1EO0 1PQV 1Y1V 1Y1Y 3GTM 3PO3
PDBsum	1ENW 1EO0 1PQV 1Y1V 1Y1Y 3GTM 3PO3
ProteinModelPortal	P07273
SMR	P07273
BioGrid	33205
DIP	DIP-2307N
IntAct	P07273
MINT	MINT-1167083
STRING	4932.YGL043W
MaxQB	P07273
PaxDb	P07273
PeptideAtlas	P07273
EnsemblFungi	[example_ID YGL043W]
GeneID	852839
KEGG	sce:YGL043W
CYGD	YGL043w
SGD	S000003011
eggNOG	COG1594
GeneTree	ENSGT00390000017794
HOGENOM	HOG000195015
InParanoid	P07273
KO	K03145
OMA	ESEHPPQ
OrthoDB	EOG7DNP5M
BioCyc	YEAST:G3O-30554-MONOMER
Reactome	REACT_235070 REACT_247354
EvolutionaryTrace	P07273
NextBio	972417
PRO	PR:P07273
Proteomes	UP000002311
Genevestigator	P07273
GO	GO:0005634 GO:0001139 GO:0000993 GO:0001012 GO:0008270 GO:0001193 GO:0006379 GO:0045899 GO:0032968 GO:0031440 GO:0051123 GO:0031564 GO:0006362 GO:0006368 GO:0006383 GO:0006367 GO:0042797
Gene3D	1.10.472.30 1.20.930.10
InterPro	IPR016492 IPR003617 IPR003618 IPR017923 IPR017890 IPR006289 IPR001222
Pfam	PF08711 PF01096 PF07500
PIRSF	PIRSF006704
SMART	SM00510 SM00509 SM00440
SUPFAM	SSF46942 SSF47676
TIGRFAMs	TIGR01385
PROSITE	PS51321 PS51319 PS00466 PS51133

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0045899	positive regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:17913884^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045899	positive regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:17913884^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042797	tRNA transcription by RNA polymerase III	PMID:18628399^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032968	positive regulation of transcription elongation from RNA polymerase II promoter	PMID:8876173^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031564	transcription antitermination	PMID:9037112^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031564	transcription antitermination	PMID:8636112^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031564	transcription antitermination	PMID:9169440^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031440	regulation of mRNA 3'-end processing	PMID:15531585^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003348	P	Seeded From UniProt	complete
involved_in	GO:0031440	regulation of mRNA 3'-end processing	PMID:15531585^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006383	transcription by RNA polymerase III	PMID:18628399^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:8288647^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:8288647^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:7020755^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:7002153^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:9334234^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:17901206^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003095	P	Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:17901206^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:15767671^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:17901206^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006362	transcription elongation from RNA polymerase I promoter	PMID:7002153^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9334234^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0001193	maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter	PMID:17535246^[14]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003038	P	Seeded From UniProt	complete
involved_in	GO:0001193	maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter	PMID:16492753^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0001193	maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter	PMID:14531857^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0001139	RNA polymerase II complex recruiting activity	PMID:15767671^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001012	RNA polymerase II regulatory region DNA binding	PMID:15767671^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:6985606^[17]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	F	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:8876173^[3]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	F	Seeded From UniProt	complete
involved_in	GO:0051123	RNA polymerase II preinitiation complex assembly	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0001139	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001222 InterPro:IPR006289	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003617 InterPro:IPR006289 InterPro:IPR017923	C	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001222 InterPro:IPR003618 InterPro:IPR006289 InterPro:IPR036575	P	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006289	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001222	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Kim, B et al. (2007) The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes. Proc. Natl. Acad. Sci. U.S.A. 104 16068-73 PubMed GONUTS page
↑ ^2.0 ^2.1 Ghavi-Helm, Y et al. (2008) Genome-wide location analysis reveals a role of TFIIS in RNA polymerase III transcription. Genes Dev. 22 1934-47 PubMed GONUTS page
↑ ^3.0 ^3.1 Wu, J et al. (1996) In vitro characterization of mutant yeast RNA polymerase II with reduced binding for elongation factor TFIIS. Proc. Natl. Acad. Sci. U.S.A. 93 11552-7 PubMed GONUTS page
↑ Powell, W et al. (1997) Glutamic acid-371 of the barnase homology domain in RNA polymerase II is not required for SII-activated RNA cleavage. Mol. Gen. Genet. 253 507-11 PubMed GONUTS page
↑ Powell, W & Reines, D (1996) Mutations in the second largest subunit of RNA polymerase II cause 6-azauracil sensitivity in yeast and increased transcriptional arrest in vitro. J. Biol. Chem. 271 6866-73 PubMed GONUTS page
↑ Awrey, DE et al. (1997) Transcription elongation through DNA arrest sites. A multistep process involving both RNA polymerase II subunit RPB9 and TFIIS. J. Biol. Chem. 272 14747-54 PubMed GONUTS page
↑ ^7.0 ^7.1 Kaplan, CD et al. (2005) Interaction between transcription elongation factors and mRNA 3'-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus. J. Biol. Chem. 280 913-22 PubMed GONUTS page
↑ ^8.0 ^8.1 Christie, KR et al. (1994) Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37. J. Biol. Chem. 269 936-43 PubMed GONUTS page
↑ Sawadogo, M et al. (1981) Native deoxyribonucleic acid transcription by yeast RNA polymerase--P37 complex. Biochemistry 20 3542-7 PubMed GONUTS page
↑ ^10.0 ^10.1 Sawadogo, M et al. (1980) Similar binding site for P37 factor on yeast RNA polymerases A and B. Biochem. Biophys. Res. Commun. 96 258-64 PubMed GONUTS page
↑ ^11.0 ^11.1 Shimoaraiso, M et al. (1997) Identification of the region in yeast S-II that defines species specificity in its interaction with RNA polymerase II. J. Biol. Chem. 272 26550-4 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Guglielmi, B et al. (2007) TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo. Proc. Natl. Acad. Sci. U.S.A. 104 16062-7 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Prather, DM et al. (2005) Evidence that the elongation factor TFIIS plays a role in transcription initiation at GAL1 in Saccharomyces cerevisiae. Mol. Cell. Biol. 25 2650-9 PubMed GONUTS page
↑ Koyama, H et al. (2007) Stimulation of RNA polymerase II transcript cleavage activity contributes to maintain transcriptional fidelity in yeast. Genes Cells 12 547-59 PubMed GONUTS page
↑ Nesser, NK et al. (2006) RNA polymerase II subunit Rpb9 is important for transcriptional fidelity in vivo. Proc. Natl. Acad. Sci. U.S.A. 103 3268-73 PubMed GONUTS page
↑ Koyama, H et al. (2003) Transcription elongation factor S-II maintains transcriptional fidelity and confers oxidative stress resistance. Genes Cells 8 779-88 PubMed GONUTS page
↑ Sawadogo, M et al. (1980) Interaction of a new polypeptide with yeast RNA polymerase B. J. Biol. Chem. 255 12-5 PubMed GONUTS page

[PMID:17913884-1] 1.0 ^1.1 Kim, B et al. (2007) The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes. Proc. Natl. Acad. Sci. U.S.A. 104 16068-73 PubMed GONUTS page

[PMID:18628399-2] 2.0 ^2.1 Ghavi-Helm, Y et al. (2008) Genome-wide location analysis reveals a role of TFIIS in RNA polymerase III transcription. Genes Dev. 22 1934-47 PubMed GONUTS page

[PMID:8876173-3] 3.0 ^3.1 Wu, J et al. (1996) In vitro characterization of mutant yeast RNA polymerase II with reduced binding for elongation factor TFIIS. Proc. Natl. Acad. Sci. U.S.A. 93 11552-7 PubMed GONUTS page

[PMID:9037112-4] Powell, W et al. (1997) Glutamic acid-371 of the barnase homology domain in RNA polymerase II is not required for SII-activated RNA cleavage. Mol. Gen. Genet. 253 507-11 PubMed GONUTS page

[PMID:8636112-5] Powell, W & Reines, D (1996) Mutations in the second largest subunit of RNA polymerase II cause 6-azauracil sensitivity in yeast and increased transcriptional arrest in vitro. J. Biol. Chem. 271 6866-73 PubMed GONUTS page

[PMID:9169440-6] Awrey, DE et al. (1997) Transcription elongation through DNA arrest sites. A multistep process involving both RNA polymerase II subunit RPB9 and TFIIS. J. Biol. Chem. 272 14747-54 PubMed GONUTS page

[PMID:15531585-7] 7.0 ^7.1 Kaplan, CD et al. (2005) Interaction between transcription elongation factors and mRNA 3'-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus. J. Biol. Chem. 280 913-22 PubMed GONUTS page

[PMID:8288647-8] 8.0 ^8.1 Christie, KR et al. (1994) Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37. J. Biol. Chem. 269 936-43 PubMed GONUTS page

[PMID:7020755-9] Sawadogo, M et al. (1981) Native deoxyribonucleic acid transcription by yeast RNA polymerase--P37 complex. Biochemistry 20 3542-7 PubMed GONUTS page

[PMID:7002153-10] 10.0 ^10.1 Sawadogo, M et al. (1980) Similar binding site for P37 factor on yeast RNA polymerases A and B. Biochem. Biophys. Res. Commun. 96 258-64 PubMed GONUTS page

[PMID:9334234-11] 11.0 ^11.1 Shimoaraiso, M et al. (1997) Identification of the region in yeast S-II that defines species specificity in its interaction with RNA polymerase II. J. Biol. Chem. 272 26550-4 PubMed GONUTS page

[PMID:17901206-12] 12.0 ^12.1 ^12.2 Guglielmi, B et al. (2007) TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo. Proc. Natl. Acad. Sci. U.S.A. 104 16062-7 PubMed GONUTS page

[PMID:15767671-13] 13.0 ^13.1 ^13.2 Prather, DM et al. (2005) Evidence that the elongation factor TFIIS plays a role in transcription initiation at GAL1 in Saccharomyces cerevisiae. Mol. Cell. Biol. 25 2650-9 PubMed GONUTS page

[PMID:17535246-14] Koyama, H et al. (2007) Stimulation of RNA polymerase II transcript cleavage activity contributes to maintain transcriptional fidelity in yeast. Genes Cells 12 547-59 PubMed GONUTS page

[PMID:16492753-15] Nesser, NK et al. (2006) RNA polymerase II subunit Rpb9 is important for transcriptional fidelity in vivo. Proc. Natl. Acad. Sci. U.S.A. 103 3268-73 PubMed GONUTS page

[PMID:14531857-16] Koyama, H et al. (2003) Transcription elongation factor S-II maintains transcriptional fidelity and confers oxidative stress resistance. Genes Cells 8 779-88 PubMed GONUTS page

[PMID:6985606-17] Sawadogo, M et al. (1980) Interaction of a new polypeptide with yeast RNA polymerase B. J. Biol. Chem. 255 12-5 PubMed GONUTS page

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YEAST:TFS2

Contents

Annotations

Notes

References

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