ESS1 peptidylprolyl isomerase ESS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: ESS1
Official Full Name: peptidylprolyl isomerase ESS1
Primary source: SGD:S000003778
Locus tag: YJR017C
See related: AllianceGenome:SGD:S000003778; FungiDB:YJR017C; VEuPathDB:YJR017C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: PIN1; PTF1
Summary: Enables RNA polymerase II complex binding activity and peptidyl-prolyl cis-trans isomerase activity. Involved in negative regulation of ubiquitin-dependent protein catabolic process; regulation of gene expression; and termination of RNA polymerase II transcription. Predicted to be located in cytoplasm. Predicted to be active in cytosol and nucleus. Orthologous to human PIN1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See ESS1 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 1

Sequence:: Chromosome: X; NC_001142.9 (466521..467033, complement)

Chromosome X - NC_001142.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.
Title: Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.
In this way, Ess1 plays an integral role in writing (and reading) the so-called CTD code to promote production of mature RNA pol II transcripts including non-coding RNAs and mRNAs.
Title: The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.
ESS1 associates with the phospho-Ser5 form of the RNA polymerase II (pol II) in vivo, is present along the entire length of coding genes, and is critical for regulating the phosphorylation of Ser7 within the pol II carboxy-terminal domain.
Title: Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle.
Cpr1 and Ess1 interact with the tombusvirus p33 and inhibit viral replication in yeast model host.
Title: Cpr1 cyclophilin and Ess1 parvulin prolyl isomerases interact with the tombusvirus replication protein and inhibit viral replication in yeast model host.
The prolyl isomerase Ess1 is required for Nrd1-dependent termination of noncoding RNAs.
Title: The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway.
Study suggests that the Pin1 activity is often translated into a fate-determining ubiquitylation switch, and that Pin1 may affect the degree of substrate ubiquitylation in other pathways as well.
Title: Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation.
The Ess1 peptidyl prolyl isomerase functionally interacts with the transcription initiation factor TFIIB and with the Ssu72 C-terminal domain phosphatase and Pta1 components of the CPF 3'-end processing complex.
Title: Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries.
analysis of an alternative catalytic mechanism for Pin1
Title: Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.
Here we report that the exonic splicing silencer (ESS1) that represses splicing of PTPRC (encoding CD45) exon 4 does not function by the typical mechanism of inhibiting binding of U1 or U2 small nuclear ribonucleoproteins (snRNPs) to the splice sites.
Title: An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition.
a level of fewer than 400 molecules per cell is sufficient for growth vs. approximately 200,000 molecules per WT cell
Title: Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II complex binding	IPI Inferred from Physical Interaction more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables peptidyl-prolyl cis-trans isomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in negative regulation of transcription by RNA polymerase II	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of transcription by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of RNA polymerase II transcription preinitiation complex assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of rDNA heterochromatin formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	IPI Inferred from Physical Interaction more info	PubMed
involved_in regulation of macromolecule metabolic process	IEA Inferred from Electronic Annotation more info
involved_in regulation of primary metabolic process	IEA Inferred from Electronic Annotation more info
involved_in termination of RNA polymerase II transcription	IGI Inferred from Genetic Interaction more info	PubMed
involved_in termination of RNA polymerase II transcription	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IC Inferred by Curator more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: peptidylprolyl isomerase ESS1

NP_012551.2

EC 5.2.1.8

Peptidylprolyl-cis/trans-isomerase (PPIase); specific for phosphorylated S/T residues N-terminal to proline; regulates phosphorylation of RNAPII large subunit (Rpo21p) C-terminal domain (CTD) at Ser7; associates with phospho-Ser5 form of RNAPII in vivo; present along entire coding length of genes; represses initiation of CUTs; required for efficient termination of mRNA transcription, trimethylation of histone H3; human ortholog PIN1 can complement yeast null and ts mutants

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001142.9 Reference assembly

Range

466521..467033 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181675.1 → NP_012551.2 TPA: peptidylprolyl isomerase ESS1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012551.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VWJ3, P22696

UniProtKB/TrEMBL

A6ZPY5, B3LQB5, C7GWK7, G2WH30, N1P8M8

Conserved Domains (2) summary

smart00456
Location:10 → 43

WW; Domain with 2 conserved Trp (W) residues

cl29122
Location:59 → 170

Rotamase_2; PPIC-type PPIASE domain