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P22696 (ESS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Peptidyl-prolyl cis-trans isomerase ESS1

Short name=PPIase ESS1
EC=5.2.1.8
Alternative name(s):
Parvulin ESS1
Processing/termination factor 1
Gene names
Name:ESS1
Synonyms:PIN1, PTF1
Ordered Locus Names:YJR017C
ORF Names:J1452
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential PPIase specific for phosphoserine and phosphothreonine N-terminal to the proline residue. Required for efficient pre-mRNA 3'-end processing and transcription termination, probably by inducing conformational changes by proline-directed isomerization in the C-terminal domain (CTD) of RPB1, thereby altering cofactor binding with the RNA polymerase II transcription complex. Also targets the SIN3-RPD3 histone deacetylase complex (HDAC).

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). Ref.6

Enzyme regulation

Inhibited by 5-hydroxy-1,4-naphthoquinone (juglone), but not by FK506 or cyclosporin A. Ref.5

Subunit structure

Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3. Ref.7 Ref.8

Subcellular location

Cytoplasm. Nucleus Ref.10.

Domain

The WW domain binds to the phosphorylated tandem 7 residues repeats of RPB1.

Miscellaneous

Present with 4401 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PpiC/parvulin rotamase family.

Contains 1 PpiC domain.

Contains 1 WW domain.

Sequence caution

The sequence CAA60941.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA89541.1 differs from that shown. Reason: Erroneous initiation.

The sequence described in Ref.1 differs from that shown. Reason: Frameshift at position 127.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Molecular functionIsomerase
Rotamase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H3-K4 trimethylation

Inferred from mutant phenotype PubMed 22778132. Source: SGD

negative regulation of histone deacetylation

Inferred from mutant phenotype Ref.8. Source: SGD

negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 19597489. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 14704159. Source: SGD

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from genetic interaction PubMed 15166139. Source: SGD

positive regulation of chromatin silencing at rDNA

Inferred from mutant phenotype Ref.8. Source: SGD

positive regulation of protein dephosphorylation

Inferred from direct assay PubMed 11904169. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 10899126. Source: SGD

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from direct assay Ref.12. Source: SGD

regulation of phosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay PubMed 22778132. Source: SGD

regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 11708797. Source: SGD

regulation of transcription involved in G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 11708797. Source: SGD

termination of RNA polymerase II transcription

Inferred from mutant phenotype PubMed 14704159PubMed 19854134PubMed 22778132. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred by curator Ref.7PubMed 10899126Ref.8PubMed 11708797PubMed 14704159. Source: SGD

   Molecular_functionRNA polymerase II core binding

Inferred from physical interaction Ref.7PubMed 10899126. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 11805826PubMed 21179020. Source: IntAct

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay Ref.12Ref.6. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-6679,EBI-6679
SSA2P105922EBI-6679,EBI-8603

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170Peptidyl-prolyl cis-trans isomerase ESS1
PRO_0000193433

Regions

Domain9 – 4335WW
Domain57 – 170114PpiC

Amino acid modifications

Modified residue1611Phosphoserine Ref.13

Experimental info

Mutagenesis1201C → R: Abolishes PPIase activity. Ref.12
Mutagenesis1221S → P: Abolishes PPIase activity. Ref.12
Mutagenesis1271G → D in PTF1-2; decreases the catalytic efficiency 20-fold. Ref.6
Mutagenesis1621G → S in PTF1-5; decreases the catalytic efficiency 12-fold. Ref.6
Mutagenesis1641H → R: Abolishes PPIase activity. Ref.12
Sequence conflict81R → S Ref.1
Sequence conflict171V → A Ref.1
Sequence conflict1281D → G Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22696 [UniParc].

Last modified October 25, 2005. Version 3.
Checksum: 18D3EC02E8395175

FASTA17019,405
        10         20         30         40         50         60 
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH KHLRDHPVRV 

        70         80         90        100        110        120 
RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR LDDDSKTNSF EALAKERSDC 

       130        140        150        160        170 
SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV GEVSDIVESG SGVHVIKRVG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae."
Hanes S.D., Shank P.R., Bostian K.A.
Yeast 5:55-72(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBY864.
[2]"PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases."
Hani J., Stumpf G., Domdey H.
FEBS Lett. 365:198-202(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DH484.
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone."
Hennig L., Christner C., Kipping M., Schelbert B., Ruecknagel K.P., Grabley S., Kuellertz G., Fischer G.
Biochemistry 37:5953-5960(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[6]"Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae."
Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G., Wiebauer K., Rahfeld J.-U.
J. Biol. Chem. 274:108-116(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-127 AND GLY-162.
[7]"Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation."
Morris D.P., Phatnani H.P., Greenleaf A.L.
J. Biol. Chem. 274:31583-31587(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RPB1.
[8]"Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase."
Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.
EMBO J. 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIN3.
[9]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae."
Gemmill T.R., Wu X., Hanes S.D.
J. Biol. Chem. 280:15510-15517(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-120; SER-122 AND HIS-164.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85972 Genomic DNA. Translation: CAA59961.1.
X87611 Genomic DNA. Translation: CAA60941.1. Different initiation.
Z49517 Genomic DNA. Translation: CAA89541.1. Different initiation.
BK006943 Genomic DNA. Translation: DAA08809.1.
PIRS52764.
RefSeqNP_012551.2. NM_001181675.1.

3D structure databases

ProteinModelPortalP22696.
SMRP22696. Positions 10-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33773. 125 interactions.
DIPDIP-3856N.
IntActP22696. 92 interactions.
MINTMINT-569771.
STRING4932.YJR017C.

Chemistry

BindingDBP22696.

Proteomic databases

PaxDbP22696.
PeptideAtlasP22696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR017C; YJR017C; YJR017C.
GeneID853475.
KEGGsce:YJR017C.

Organism-specific databases

CYGDYJR017c.
SGDS000003778. ESS1.

Phylogenomic databases

eggNOGCOG0760.
GeneTreeENSGT00640000091578.
HOGENOMHOG000275331.
KOK09578.
OMAGRGEMQP.
OrthoDBEOG7HHX51.

Enzyme and pathway databases

BioCycYEAST:YJR017C-MONOMER.

Gene expression databases

GenevestigatorP22696.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974080.
PROP22696.

Entry information

Entry nameESS1_YEAST
AccessionPrimary (citable) accession number: P22696
Secondary accession number(s): D6VWJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 25, 2005
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families