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P07273 (TFS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription elongation factor S-II
Alternative name(s):
DNA strand transfer protein alpha
Short name=STP-alpha
DNA strand transferase 1
Pyrimidine pathway regulatory protein 2
Gene names
Name:DST1
Synonyms:PPR2
Ordered Locus Names:YGL043W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.

Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.

Subcellular location

Nucleus.

Miscellaneous

S-II binds to RNA-polymerase II in the absence of transcription.

Present with 6260 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TFS-II family.

Contains 1 TFIIS central domain.

Contains 1 TFIIS N-terminal domain.

Contains 1 TFIIS-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polymerase II transcriptional preinitiation complex assembly

Inferred from mutant phenotype PubMed 15767671. Source: GOC

mRNA cleavage

Inferred from direct assay PubMed 12692127. Source: SGD

maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 14531857PubMed 16492753. Source: SGD

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from direct assay PubMed 17913884. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 8876173. Source: SGD

regulation of mRNA 3'-end processing

Inferred from mutant phenotype PubMed 15531585. Source: SGD

tRNA transcription from RNA polymerase III promoter

Inferred from mutant phenotype PubMed 18628399. Source: SGD

transcription antitermination

Inferred from direct assay PubMed 8636112PubMed 9037112PubMed 9169440. Source: SGD

transcription elongation from RNA polymerase I promoter

Inferred from direct assay PubMed 7002153. Source: SGD

transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 7002153PubMed 7020755PubMed 8288647PubMed 9334234. Source: SGD

transcription from RNA polymerase III promoter

Inferred from direct assay PubMed 18628399. Source: SGD

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 17901206. Source: SGD

   Cellular_componentnucleus

Inferred from direct assay PubMed 9334234. Source: SGD

   Molecular_functionRNA polymerase II core binding

Inferred from physical interaction PubMed 6985606PubMed 8876173. Source: SGD

RNA polymerase II regulatory region DNA binding

Inferred from direct assay PubMed 15767671. Source: SGD

core RNA polymerase II recruiting transcription factor activity

Inferred from mutant phenotype PubMed 15767671. Source: SGD

protein binding

Inferred from physical interaction PubMed 21057455. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SPT8P389152EBI-19168,EBI-17964
SSN2P389312EBI-19168,EBI-18059

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Transcription elongation factor S-II
PRO_0000121443

Regions

Domain5 – 7975TFIIS N-terminal
Domain148 – 264117TFIIS central
Zinc finger267 – 30741TFIIS-type

Amino acid modifications

Modified residue1161Phosphoserine Ref.11

Experimental info

Sequence conflict351V → F in AAA88734. Ref.1
Sequence conflict351V → F in AAA34580. Ref.1
Sequence conflict74 – 774DAIN → AQLI in AAA88734. Ref.1
Sequence conflict74 – 774DAIN → AQLI in AAA34580. Ref.1
Sequence conflict821S → C in AAA88734. Ref.1
Sequence conflict821S → C in AAA34580. Ref.1
Sequence conflict851A → P in AAA88734. Ref.1
Sequence conflict851A → P in AAA34580. Ref.1

Secondary structure

......................................... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07273 [UniParc].

Last modified October 1, 1996. Version 4.
Checksum: D133938319C015FF

FASTA30934,843
        10         20         30         40         50         60 
MDSKEVLVHV KNLEKNKSND AAVLEILHVL DKEFVPTEKL LRETKVGVEV NKFKKSTNVE 

        70         80         90        100        110        120 
ISKLVKKMIS SWKDAINKNK RSRQAQQHHQ DHAPGNAEDK TTVGESVNGV QQPASSQSDA 

       130        140        150        160        170        180 
MKQDKYVSTK PRNSKNDGVD TAIYHHKLRD QVLKALYDVL AKESEHPPQS ILHTAKAIES 

       190        200        210        220        230        240 
EMNKVNNCDT NEAAYKARYR IIYSNVISKN NPDLKHKIAN GDITPEFLAT CDAKDLAPAP 

       250        260        270        280        290        300 
LKQKIEEIAK QNLYNAQGAT IERSVTDRFT CGKCKEKKVS YYQLQTRSAD EPLTTFCTCE 


ACGNRWKFS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, DNA sequence, and regulation of a Saccharomyces cerevisiae gene that encodes DNA strand transfer protein alpha."
Clark A.B., Dykstra C.C., Sugino A.
Mol. Cell. Biol. 11:2576-2582(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-30.
[2]"Purification, gene cloning, and gene disruption of the transcription elongation factor S-II in Saccharomyces cerevisiae."
Nakanishi T., Nakano A., Sekimizu K., Natori S.
J. Biol. Chem. 267:13200-13204(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Complete sequence of a eukaryotic regulatory gene."
Hubert J.-C., Guyonvarch A., Kammerer B., Exinger F., Liljelund P., Lacroute F.
EMBO J. 2:2071-2073(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-309.
[7]"Homologue of TFIIS in yeast."
Davies C.J., Trgovchich J., Hutchison C.A. III
Nature 345:298-298(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO S-II.
[8]"TFIIS and strand-transfer proteins."
Kipling D., Kearsey S.E.
Nature 353:509-509(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTITY OF PPR2 AND DST1.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36724 Genomic DNA. Translation: AAA88734.1.
D12478 Genomic DNA. Translation: BAA02046.1.
M60770 Genomic DNA. Translation: AAA34580.1.
Z72565 Genomic DNA. Translation: CAA96744.1.
X00047 Genomic DNA. Translation: CAA24928.1.
BK006941 Genomic DNA. Translation: DAA08057.1.
PIRA42921.
RefSeqNP_011472.1. NM_001180908.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ENWNMR-A131-240[»]
1EO0NMR-A1-77[»]
1PQVX-ray3.80S1-309[»]
1Y1VX-ray3.80S131-309[»]
1Y1YX-ray4.00S131-309[»]
3GTMX-ray3.80S147-309[»]
3PO3X-ray3.30S132-309[»]
ProteinModelPortalP07273.
SMRP07273. Positions 1-77, 147-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33205. 273 interactions.
DIPDIP-2307N.
IntActP07273. 6 interactions.
MINTMINT-1167083.
STRING4932.YGL043W.

Proteomic databases

MaxQBP07273.
PaxDbP07273.
PeptideAtlasP07273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL043W; YGL043W; YGL043W.
GeneID852839.
KEGGsce:YGL043W.

Organism-specific databases

CYGDYGL043w.
SGDS000003011. DST1.

Phylogenomic databases

eggNOGCOG1594.
GeneTreeENSGT00390000017794.
HOGENOMHOG000195015.
KOK03145.
OMAVNIYSAV.
OrthoDBEOG7DNP5M.

Enzyme and pathway databases

BioCycYEAST:G3O-30554-MONOMER.

Gene expression databases

GenevestigatorP07273.

Family and domain databases

Gene3D1.10.472.30. 1 hit.
1.20.930.10. 1 hit.
InterProIPR016492. TF_IIS-rel.
IPR003617. TFIIS/CRSP70_N_sub.
IPR003618. TFIIS_cen_dom.
IPR017923. TFIIS_N.
IPR017890. TFS2M.
IPR006289. TFSII.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamPF08711. Med26. 1 hit.
PF01096. TFIIS_C. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]
PIRSFPIRSF006704. TF_IIS. 1 hit.
SMARTSM00510. TFS2M. 1 hit.
SM00509. TFS2N. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]
SUPFAMSSF46942. SSF46942. 1 hit.
SSF47676. SSF47676. 1 hit.
TIGRFAMsTIGR01385. TFSII. 1 hit.
PROSITEPS51321. TFIIS_CENTRAL. 1 hit.
PS51319. TFIIS_N. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07273.
NextBio972417.
PROP07273.

Entry information

Entry nameTFS2_YEAST
AccessionPrimary (citable) accession number: P07273
Secondary accession number(s): D6VU96, P24535
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references