P22696 (ESS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

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):
Parvulin ESS1
Processing/termination factor 1

Gene names

Name:	ESS1
Synonyms:	PIN1, PTF1
Ordered Locus Names:	YJR017C
ORF Names:	J1452

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
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.6
Enzyme regulation	Inhibited by 5-hydroxy-1,4-naphthoquinone (juglone), but not by FK506 or cyclosporin A. Ref.5
Subunit structure	Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3. Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus Ref.10.
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.
Sequence similarities	Belongs to the PpiC/parvulin rotamase family. Contains 1 PpiC domain. Contains 1 WW domain.
Sequence caution	The sequence CAA60941.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA89541.1 differs from that shown. Reason: Erroneous initiation. The sequence described in Ref.1 differs from that shown. Reason: Frameshift at position 127.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of histone deacetylation Inferred from mutant phenotype Ref.8. Source: SGD negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype PubMed 19597489. Source: SGD negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 14704159. Source: SGD positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from genetic interaction PubMed 15166139. Source: SGD positive regulation of chromatin silencing at rDNA Inferred from mutant phenotype Ref.8. Source: SGD positive regulation of protein dephosphorylation Inferred from direct assay PubMed 11904169. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription involved in G1 phase of mitotic cell cycle Inferred from mutant phenotype PubMed 11708797. Source: SGD regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from mutant phenotype PubMed 11708797. Source: SGD termination of RNA polymerase II transcription Inferred from mutant phenotype PubMed 14704159PubMed 19854134. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred by curator Ref.7PubMed 10899126Ref.8PubMed 11708797PubMed 14704159. Source: SGD
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.12Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-6679,EBI-6679
BCY1	P07278	2	EBI-6679,EBI-9475
SSA2	P10592	2	EBI-6679,EBI-8603

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.13
	Modified residue	140	1	Phosphoserine Ref.13
	Modified residue	161	1	Phosphoserine Ref.13
Experimental info
	Mutagenesis	120	1	C → R: Abolishes PPIase activity. Ref.12
	Mutagenesis	122	1	S → P: Abolishes PPIase activity. Ref.12
	Mutagenesis	127	1	G → D in PTF1-2; decreases the catalytic efficiency 20-fold. Ref.6
	Mutagenesis	162	1	G → S in PTF1-5; decreases the catalytic efficiency 12-fold. Ref.6
	Mutagenesis	164	1	H → R: Abolishes PPIase activity. Ref.12
	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

	Sequence		Length	Mass (Da)
	P22696 [UniParc]. Last modified October 25, 2005. Version 3. Checksum: 18D3EC02E8395175	FASTA	170	19,405
	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

References

	« Hide 'large scale' referencesShow '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] [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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"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] [Europe PMC] [Abstract] 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-109; SER-140 AND SER-161, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S52764.
RefSeq	NP_012551.2. NM_001181675.1.
3D structure databases
ProteinModelPortal	P22696.
SMR	P22696. Positions 11-170.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3856N.
IntAct	P22696. 107 interactions.
MINT	MINT-569771.
STRING	4932.YJR017C.
Proteomic databases
PaxDb	P22696.
PeptideAtlas	P22696.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJR017C; YJR017C; YJR017C.
GeneID	853475.
KEGG	sce:YJR017C.
Organism-specific databases
CYGD	YJR017c.
SGD	S000003778. ESS1.
Phylogenomic databases
eggNOG	COG0760.
GeneTree	ENSGT00640000091578.
HOGENOM	HOG000275331.
KO	K09578.
OMA	GRGEMQP.
OrthoDB	EOG4FJCK9.
Gene expression databases
Genevestigator	P22696.
GermOnline	YJR017C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000297. PPIase_PpiC. IPR023058. PPIase_PpiC_CS. IPR001202. WW_dom. [Graphical view]
Pfam	PF00639. Rotamase. 1 hit. PF00397. WW. 1 hit. [Graphical view]
SMART	SM00456. WW. 1 hit. [Graphical view]
SUPFAM	SSF51045. WW_Rsp5_WWP. 1 hit.
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
BindingDB	P22696.
NextBio	974080.

Entry information

Entry name

ESS1_YEAST

Accession

Primary (citable) accession number: P22696
Secondary accession number(s): D6VWJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program