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P22696

- ESS1_YEAST

UniProt

P22696 - ESS1_YEAST

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Protein

Peptidyl-prolyl cis-trans isomerase ESS1

Gene
ESS1, PIN1, PTF1, YJR017C, J1452
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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. protein binding Source: IntAct
  4. 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 folding Source: UniProtKB-KW
  10. protein peptidyl-prolyl isomerization Source: SGD
  11. regulation of phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  12. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
  13. regulation of transcription involved in G2/M transition of mitotic cell cycle Source: SGD
  14. 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: Chromosome X

Organism-specific databases

CYGDiYJR017c.
SGDiS000003778. ESS1.

Subcellular locationi

Cytoplasm. 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. 126 interactions.
DIPiDIP-3856N.
IntActiP22696. 92 interactions.
MINTiMINT-569771.
STRINGi4932.YJR017C.

Structurei

3D structure databases

ProteinModelPortaliP22696.
SMRiP22696. Positions 11-170.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 4335WWAdd
BLAST
Domaini57 – 170114PpiCAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 PpiC domain.
Contains 1 WW domain.

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
KOiK09578.
OMAiCLHLLIK.
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

MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH    50
KHLRDHPVRV RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR 100
LDDDSKTNSF EALAKERSDC SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV 150
GEVSDIVESG SGVHVIKRVG 170
Length:170
Mass (Da):19,405
Last modified:October 25, 2005 - v3
Checksum:i18D3EC02E8395175
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81R → S1 Publication
Sequence conflicti17 – 171V → A1 Publication
Sequence conflicti128 – 1281D → G1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S52764.
RefSeqi NP_012551.2. NM_001181675.1.

3D structure databases

ProteinModelPortali P22696.
SMRi P22696. Positions 11-170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33773. 126 interactions.
DIPi DIP-3856N.
IntActi P22696. 92 interactions.
MINTi MINT-569771.
STRINGi 4932.YJR017C.

Chemistry

BindingDBi P22696.

Proteomic databases

MaxQBi P22696.
PaxDbi P22696.
PeptideAtlasi P22696.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR017C ; YJR017C ; YJR017C .
GeneIDi 853475.
KEGGi sce:YJR017C.

Organism-specific databases

CYGDi YJR017c.
SGDi S000003778. ESS1.

Phylogenomic databases

eggNOGi COG0760.
GeneTreei ENSGT00640000091578.
HOGENOMi HOG000275331.
KOi K09578.
OMAi CLHLLIK.
OrthoDBi EOG7HHX51.

Enzyme and pathway databases

BioCyci YEAST:YJR017C-MONOMER.

Miscellaneous databases

NextBioi 974080.
PROi P22696.

Gene expression databases

Genevestigatori P22696.

Family and domain databases

InterProi IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS01096. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 138 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.

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