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Protein

Peptidyl-prolyl cis-trans isomerase ESS1

Gene

ESS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

Enzyme regulationi

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

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. peptidyl-prolyl cis-trans isomerase activity Source: SGD
  3. RNA polymerase II core binding Source: SGD

GO - Biological processi

  1. histone H3-K4 trimethylation Source: SGD
  2. negative regulation of histone deacetylation Source: SGD
  3. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  4. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  5. positive regulation of chromatin silencing at rDNA Source: SGD
  6. positive regulation of protein dephosphorylation Source: SGD
  7. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  8. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  9. protein peptidyl-prolyl isomerization Source: SGD
  10. regulation of phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  11. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
  12. regulation of transcription involved in G2/M transition of mitotic cell cycle Source: SGD
  13. termination of RNA polymerase II transcription Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YJR017C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase ESS1 (EC:5.2.1.8)
Short name:
PPIase ESS1
Alternative name(s):
Parvulin ESS1
Processing/termination factor 1
Gene namesi
Name:ESS1
Synonyms:PIN1, PTF1
Ordered Locus Names:YJR017C
ORF Names:J1452
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

CYGDiYJR017c.
EuPathDBiFungiDB:YJR017C.
SGDiS000003778. ESS1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201C → R: Abolishes PPIase activity. 1 Publication
Mutagenesisi122 – 1221S → P: Abolishes PPIase activity. 1 Publication
Mutagenesisi127 – 1271G → D in PTF1-2; decreases the catalytic efficiency 20-fold. 1 Publication
Mutagenesisi162 – 1621G → S in PTF1-5; decreases the catalytic efficiency 12-fold. 1 Publication
Mutagenesisi164 – 1641H → R: Abolishes PPIase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Peptidyl-prolyl cis-trans isomerase ESS1PRO_0000193433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22696.
PaxDbiP22696.
PeptideAtlasiP22696.

Expressioni

Gene expression databases

GenevestigatoriP22696.

Interactioni

Subunit structurei

Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6679,EBI-6679
SSA2P105922EBI-6679,EBI-8603

Protein-protein interaction databases

BioGridi33773. 506 interactions.
DIPiDIP-3856N.
IntActiP22696. 92 interactions.
MINTiMINT-569771.
STRINGi4932.YJR017C.

Structurei

3D structure databases

ProteinModelPortaliP22696.
SMRiP22696. Positions 11-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 4335WWPROSITE-ProRule annotationAdd
BLAST
Domaini57 – 170114PpiCPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the PpiC/parvulin rotamase family.Curated
Contains 1 PpiC domain.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
InParanoidiP22696.
KOiK09578.
OMAiGRGEMQP.
OrthoDBiEOG7HHX51.

Family and domain databases

InterProiIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01096. 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]

Sequencei

Sequence statusi: Complete.

P22696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH
60 70 80 90 100
KHLRDHPVRV RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR
110 120 130 140 150
LDDDSKTNSF EALAKERSDC SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV
160 170
GEVSDIVESG SGVHVIKRVG
Length:170
Mass (Da):19,405
Last modified:October 25, 2005 - v3
Checksum:i18D3EC02E8395175
GO

Sequence cautioni

The sequence CAA60941.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA89541.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence described in PubMed:2648698 differs from that shown. Reason: Frameshift at position 127. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81R → S (PubMed:2648698).Curated
Sequence conflicti17 – 171V → A (PubMed:2648698).Curated
Sequence conflicti128 – 1281D → G (PubMed:2648698).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS52764.
RefSeqiNP_012551.2. NM_001181675.1.

Genome annotation databases

EnsemblFungiiYJR017C; YJR017C; YJR017C.
GeneIDi853475.
KEGGisce:YJR017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS52764.
RefSeqiNP_012551.2. NM_001181675.1.

3D structure databases

ProteinModelPortaliP22696.
SMRiP22696. Positions 11-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33773. 506 interactions.
DIPiDIP-3856N.
IntActiP22696. 92 interactions.
MINTiMINT-569771.
STRINGi4932.YJR017C.

Chemistry

BindingDBiP22696.

Proteomic databases

MaxQBiP22696.
PaxDbiP22696.
PeptideAtlasiP22696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR017C; YJR017C; YJR017C.
GeneIDi853475.
KEGGisce:YJR017C.

Organism-specific databases

CYGDiYJR017c.
EuPathDBiFungiDB:YJR017C.
SGDiS000003778. ESS1.

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
InParanoidiP22696.
KOiK09578.
OMAiGRGEMQP.
OrthoDBiEOG7HHX51.

Enzyme and pathway databases

BioCyciYEAST:YJR017C-MONOMER.

Miscellaneous databases

NextBioi974080.
PROiP22696.

Gene expression databases

GenevestigatoriP22696.

Family and domain databases

InterProiIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01096. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. 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].

Entry informationi

Entry nameiESS1_YEAST
AccessioniPrimary (citable) accession number: P22696
Secondary accession number(s): D6VWJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 25, 2005
Last modified: April 29, 2015
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4401 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.