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P22696

- ESS1_YEAST

UniProt

P22696 - ESS1_YEAST

Protein

Peptidyl-prolyl cis-trans isomerase ESS1

Gene

ESS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (25 Oct 2005)
      Previous versions | rss
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    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

    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 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: SGD

    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.
    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 139 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