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UniProtKB/Swiss-Prot entry P22696

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ESS1_YEAST
Primary accession number P22696
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on October 25, 2005 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 81)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase ESS1
Synonyms PPIase ESS1
EC 5.2.1.8
Processing/termination factor 1
Parvulin ESS1
Gene name
Name: ESS1
Synonyms: PIN1, PTF1
OrderedLocusNames: YJR017C
ORFNames: J1452
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBY864;
DOI=10.1002/yea.320050108; PubMed=2648698 [NCBI, ExPASy, EBI, Israel, Japan]
Hanes S.D., Shank P.R., Bostian K.A.;
"Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae.";
Yeast 5:55-72(1989).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DH484;
DOI=10.1016/0014-5793(95)00471-K; PubMed=7781779 [NCBI, ExPASy, EBI, Israel, Japan]
Hani J., Stumpf G., Domdey H.;
"PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases.";
FEBS Lett. 365:198-202(1995).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[4]
 ENZYME REGULATION.
DOI=10.1021/bi973162p; PubMed=9558330 [NCBI, ExPASy, EBI, Israel, Japan]
Hennig L., Christner C., Kipping M., Schelbert B., Ruecknagel K.P., Grabley S., Kuellertz G., Fischer G.;
"Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone.";
Biochemistry 37:5953-5960(1998).
[5]
 CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-127 AND GLY-162.
DOI=10.1074/jbc.274.1.108; PubMed=9867817 [NCBI, ExPASy, EBI, Israel, Japan]
Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G., Wiebauer K., Rahfeld J.-U.;
"Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae.";
J. Biol. Chem. 274:108-116(1999).
[6]
 IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RPB1.
DOI=10.1074/jbc.274.44.31583; PubMed=10531363 [NCBI, ExPASy, EBI, Israel, Japan]
Morris D.P., Phatnani H.P., Greenleaf A.L.;
"Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation.";
J. Biol. Chem. 274:31583-31587(1999).
[7]
 INTERACTION WITH SIN3.
DOI=10.1093/emboj/19.14.3739; PubMed=10899127 [NCBI, ExPASy, EBI, Israel, Japan]
Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
"Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase.";
EMBO J. 19:3739-3749(2000).
[8]
 IDENTIFICATION OF PROBABLE INITIATION SITE.
DOI=10.1038/nature01644; PubMed=12748633 [NCBI, ExPASy, EBI, Israel, Japan]
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and regulatory elements.";
Nature 423:241-254(2003).
[9]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
 MUTAGENESIS OF CYS-120; SER-122 AND HIS-164.
DOI=10.1074/jbc.M412172200; PubMed=15728580 [NCBI, ExPASy, EBI, Israel, Japan]
Gemmill T.R., Wu X., Hanes S.D.;
"Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.";
J. Biol. Chem. 280:15510-15517(2005).
[12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-140 AND SER-161, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X85972; CAA59961.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X87611; CAA60941.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49517; CAA89541.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S52764; S52764.
RefSeq NP_012551.2; -.
3D structure databases
HSSP Q9SL42; 1J6Y. [HSSP ENTRY / PDB]
ModBase P22696.
Protein-protein interaction databases
DIP DIP:3856N; -.
IntAct P22696; -.
Organism-specific databases
CYGD YJR017c; -.
SGD S000003778; ESS1.
Yeast-GFP YJR017C.
Gene expression databases
GermOnline YJR017C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003711; Molecular function: transcription elongation regulator activity (inferred from genetic interaction from SGD).
GO:0006397; Biological process: mRNA processing (inferred from mutant phenotype from SGD).
GO:0042326; Biological process: negative regulation of phosphorylation (inferred from direct assay from SGD).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from genetic interaction from SGD).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
GO:0006369; Biological process: termination of RNA polymerase II transcription (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000297; PPIase_PpiC.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00639; Rotamase; 1.
PF00397; WW; 1.
Pfam graphical view of domain structure.
SMART SM00456; WW; 1.
SMART graphical view of domain structure.
PROSITE PS01096; PPIC_PPIASE_1; 1.
PS50198; PPIC_PPIASE_2; 1.
PS01159; WW_DOMAIN_1; 1.
PS50020; WW_DOMAIN_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P22696.
Proteomic databases
PeptideAtlas P22696; -.
Genome annotation databases
Ensembl YJR017C; Saccharomyces cerevisiae. [Contig view]
GeneID 853475; -.
GenomeReviews Y13136_GR; YJR017C.
KEGG sce:YJR017C; -.
NMPDR fig|4932.3.peg.3525; -.
Phylogenomic databases
HOGENOM P22696; -.
Other
LinkHub P22696; -.
NextBio 974080; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   170  170     Peptidyl-prolyl cis-trans isomerase ESS1. PRO_0000193433
DOMAIN   9    43  35     WW. 
DOMAIN   57   170  114     PpiC. 
MOD_RES   109   109        Phosphoserine. 
MOD_RES   140   140        Phosphoserine. 
MOD_RES   161   161        Phosphoserine. 
MUTAGEN   120   120        C->R: Abolishes PPIase activity. 
MUTAGEN   122   122        S->P: Abolishes PPIase activity. 
MUTAGEN   127   127        G->D: In PTF1-2; decreases the catalytic efficiency 20-fold. 
MUTAGEN   162   162        G->S: In PTF1-5; decreases the catalytic efficiency 12-fold. 
MUTAGEN   164   164        H->R: Abolishes PPIase activity. 
CONFLICT   8     8        R -> S (in Ref. 1). 
CONFLICT   17    17        V -> A (in Ref. 1). 
CONFLICT   128   128        D -> G (in Ref. 1). 
Sequence information
Length: 170 AA [This is the length of the unprocessed precursor] Molecular weight: 19405 Da [This is the MW of the unprocessed precursor] CRC64: 18D3EC02E8395175 [This is a checksum on the sequence] 
        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
P22696 in FASTA format

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