Reviewed,
UniProtKB/Swiss-Prot P22696 (ESS1_YEAST)
Last modified
June 16, 2009.
Version 86.
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90%,
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Peptidyl-prolyl cis-trans isomerase ESS1 Short name=PPIase ESS1 EC=5.2.1.8 Alternative name(s): Processing/termination factor 1 Parvulin ESS1 | ||||||||
| Gene names |
| ||||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 170 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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.5 |
| Enzyme regulation | Inhibited by 5-hydroxy-1,4-naphthoquinone (juglone), but not by FK506 or cyclosporin A. Ref.4 |
| Subunit structure | Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3. Ref.6 Ref.7 |
| Subcellular location | |
| 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. Ref.10 |
| Sequence similarities | Belongs to the ppiC/parvulin rotamase family. Contains 1 PpiC domain. Contains 1 WW domain. |
| Sequence caution | The sequence described in Ref.1 differs from that shown. Reason: Frameshift at position 127. |
Ontologies
Binary interactions
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 170 | 170 | Peptidyl-prolyl cis-trans isomerase ESS1 | PRO_0000193433 | |||||
Regions | |||||||||
| Domain | 9 – 43 | 35 | WW | ||||||
| Domain | 57 – 170 | 114 | PpiC | ||||||
Amino acid modifications | |||||||||
| Modified residue | 109 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 140 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 161 | 1 | Phosphoserine Ref.12 | ||||||
Experimental info | |||||||||
| Mutagenesis | 120 | 1 | C → R: Abolishes PPIase activity. Ref.11 | ||||||
| Mutagenesis | 122 | 1 | S → P: Abolishes PPIase activity. Ref.11 | ||||||
| Mutagenesis | 127 | 1 | G → D in PTF1-2; decreases the catalytic efficiency 20-fold. Ref.5 | ||||||
| Mutagenesis | 162 | 1 | G → S in PTF1-5; decreases the catalytic efficiency 12-fold. Ref.5 | ||||||
| Mutagenesis | 164 | 1 | H → R: Abolishes PPIase activity. Ref.11 | ||||||
| Sequence conflict | 8 | 1 | R → S Ref.1 | ||||||
| Sequence conflict | 17 | 1 | V → A Ref.1 | ||||||
| Sequence conflict | 128 | 1 | D → G Ref.1 | ||||||
Sequences
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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: 2648698] [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: 7781779] [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.  Karpfinger-Hartl L.EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | "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: 9558330] [Abstract] Cited for: ENZYME REGULATION. |
| [5] | "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: 9867817] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-127 AND GLY-162. |
| [6] | "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: 10531363] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RPB1. |
| [7] | "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: 10899127] [Abstract] Cited for: INTERACTION WITH SIN3. |
| [8] | "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: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE. |
| [9] | "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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [10] | "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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [11] | "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: 15728580] [Abstract] Cited for: MUTAGENESIS OF CYS-120; SER-122 AND HIS-164. |
| [12] | "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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-140 AND SER-161, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X85972 Genomic DNA. Translation: CAA59961.1. X87611 Genomic DNA. Translation: CAA60941.1. Different initiation. Z49517 Genomic DNA. Translation: CAA89541.1. Different initiation. | |
| PIR | S52764. |
| RefSeq | NP_012551.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J6Y based on UniProtKB Q9SL42. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:3856N. |
| IntAct | P22696. 90 interactions. |
Proteomic databases | |
| PeptideAtlas | P22696. |
Genome annotation databases | |
| Ensembl | YJR017C. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 853475. |
| GenomeReviews | Gene locus YJR017C in contig Y13136_GR. |
| KEGG | sce:YJR017C. |
| NMPDR | fig|4932.3.peg.3525. |
Organism-specific databases | |
| CYGD | YJR017c. |
| SGD | S000003778. ESS1. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P22696. |
| OMA | P22696. EMQPSFE. |
Enzyme and pathway databases | |
| BRENDA | 5.2.1.8. 250. |
Gene expression databases | |
| GermOnline | YJR017C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR000297. PPIase_PpiC. IPR001202. WW_Rsp5_WWP. [Graphical view] |
| Pfam | PF00639. Rotamase. 1 hit. PF00397. WW. 1 hit. [Graphical view] |
| SMART | SM00456. WW. 1 hit. [Graphical view] |
| PROSITE | 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] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 974080. |
Entry information
| Entry name | ESS1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P22696 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome X Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names |
