Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase ESS1

Gene

ESS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

  • peptidyl-prolyl cis-trans isomerase activity Source: SGD
  • RNA polymerase II core binding Source: SGD

GO - Biological processi

  • histone H3-K4 trimethylation Source: SGD
  • negative regulation of histone deacetylation Source: SGD
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of chromatin silencing at rDNA Source: SGD
  • positive regulation of protein dephosphorylation Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • protein peptidyl-prolyl isomerization Source: SGD
  • regulation of phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
  • regulation of transcription involved in G2/M transition of mitotic cell cycle Source: SGD
  • termination of RNA polymerase II transcription Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YJR017C-MONOMER.
ReactomeiR-SCE-6811555. PI5P Regulates TP53 Acetylation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR017C.
SGDiS000003778. ESS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi120C → R: Abolishes PPIase activity. 1 Publication1
Mutagenesisi122S → P: Abolishes PPIase activity. 1 Publication1
Mutagenesisi127G → D in PTF1-2; decreases the catalytic efficiency 20-fold. 1 Publication1
Mutagenesisi162G → S in PTF1-5; decreases the catalytic efficiency 12-fold. 1 Publication1
Mutagenesisi164H → R: Abolishes PPIase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001934331 – 170Peptidyl-prolyl cis-trans isomerase ESS1Add BLAST170

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei161PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22696.
PRIDEiP22696.
TopDownProteomicsiP22696.

PTM databases

iPTMnetiP22696.

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

GO - Molecular functioni

  • RNA polymerase II core binding Source: SGD

Protein-protein interaction databases

BioGridi33773. 507 interactors.
DIPiDIP-3856N.
IntActiP22696. 92 interactors.
MINTiMINT-569771.

Chemistry databases

BindingDBiP22696.

Structurei

3D structure databases

ProteinModelPortaliP22696.
SMRiP22696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 43WWPROSITE-ProRule annotationAdd BLAST35
Domaini57 – 170PpiCPROSITE-ProRule annotationAdd BLAST114

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

GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
InParanoidiP22696.
KOiK09578.
OMAiPWTVRYS.
OrthoDBiEOG092C4TRA.

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

        10         20         30         40         50
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH
60 70 80 90 100
KHLRDHPVRV RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR
110 120 130 140 150
LDDDSKTNSF EALAKERSDC SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV
160 170
GEVSDIVESG SGVHVIKRVG
Length:170
Mass (Da):19,405
Last modified:October 25, 2005 - v3
Checksum:i18D3EC02E8395175
GO

Sequence cautioni

The sequence CAA60941 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA89541 differs from that shown. Reason: Erroneous initiation.Curated
The sequence described in PubMed:2648698 differs from that shown. Reason: Frameshift at position 127.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8R → S (PubMed:2648698).Curated1
Sequence conflicti17V → A (PubMed:2648698).Curated1
Sequence conflicti128D → G (PubMed:2648698).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP22696.
SMRiP22696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33773. 507 interactors.
DIPiDIP-3856N.
IntActiP22696. 92 interactors.
MINTiMINT-569771.

Chemistry databases

BindingDBiP22696.

PTM databases

iPTMnetiP22696.

Proteomic databases

MaxQBiP22696.
PRIDEiP22696.
TopDownProteomicsiP22696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR017C; YJR017C; YJR017C.
GeneIDi853475.
KEGGisce:YJR017C.

Organism-specific databases

EuPathDBiFungiDB:YJR017C.
SGDiS000003778. ESS1.

Phylogenomic databases

GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
InParanoidiP22696.
KOiK09578.
OMAiPWTVRYS.
OrthoDBiEOG092C4TRA.

Enzyme and pathway databases

BioCyciYEAST:YJR017C-MONOMER.
ReactomeiR-SCE-6811555. PI5P Regulates TP53 Acetylation.

Miscellaneous databases

PROiP22696.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.