YEAST:ESS1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	ESS1 (synonyms: PIN1, PTF1)
Protein Name(s)	Peptidyl-prolyl cis-trans isomerase ESS1 PPIase ESS1 Parvulin ESS1 Processing/termination factor 1
External Links
UniProt	P22696
EMBL	X85972 X87611 Z49517 BK006943
PIR	S52764
RefSeq	NP_012551.2
ProteinModelPortal	P22696
SMR	P22696
BioGrid	33773
DIP	DIP-3856N
IntAct	P22696
MINT	MINT-569771
STRING	4932.YJR017C
BindingDB	P22696
MaxQB	P22696
PaxDb	P22696
PeptideAtlas	P22696
EnsemblFungi	[example_ID YJR017C]
GeneID	853475
KEGG	sce:YJR017C
CYGD	YJR017c
SGD	S000003778
eggNOG	COG0760
GeneTree	ENSGT00640000091578
HOGENOM	HOG000275331
InParanoid	P22696
KO	K09578
OMA	GRGEMQP
OrthoDB	EOG7HHX51
BioCyc	YEAST:YJR017C-MONOMER
NextBio	974080
PRO	PR:P22696
Proteomes	UP000002311
Genevestigator	P22696
GO	GO:0005737 GO:0005634 GO:0042802 GO:0003755 GO:0000993 GO:0080182 GO:0031064 GO:2000059 GO:0000122 GO:2000749 GO:0035307 GO:0045899 GO:0045944 GO:0000413 GO:1901407 GO:0000083 GO:0000117 GO:0006369
InterPro	IPR000297 IPR023058 IPR001202
Pfam	PF00639 PF00397
SMART	SM00456
SUPFAM	SSF51045
PROSITE	PS01096 PS50198 PS01159 PS50020

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0030052	parvulin	PMID:24468661^[1]	ECO:0000314			F	Accelerate the initial velocity of the cis-trans conversion of peptidly-prolyl bonds of a tetra peptide in a GhPPI concentration-dependent manner	complete CACAO 10586
involved_in	GO:2000749	positive regulation of chromatin silencing at rDNA	PMID:10899127^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:2000059	negative regulation of ubiquitin-dependent protein catabolic process	PMID:19597489^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1901407	regulation of phosphorylation of RNA polymerase II C-terminal domain	PMID:22778132^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0080182	histone H3-K4 trimethylation	PMID:22778132^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003880	P	Seeded From UniProt	complete
involved_in	GO:0080182	histone H3-K4 trimethylation	PMID:22778132^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:10899126^[5]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:10899126^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001083	P	Seeded From UniProt	complete
involved_in	GO:0045899	positive regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:15166139^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005963	P	Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	PMID:19854134^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	PMID:11904169^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031064	negative regulation of histone deacetylation	PMID:10899127^[2]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000004876 SGD:S000005274	P	Seeded From UniProt	complete
involved_in	GO:0031064	negative regulation of histone deacetylation	PMID:10899127^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006369	termination of RNA polymerase II transcription	PMID:19854134^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002636 SGD:S000005195	P	Seeded From UniProt	complete
involved_in	GO:0006369	termination of RNA polymerase II transcription	PMID:22778132^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006369	termination of RNA polymerase II transcription	PMID:14704159^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006369	termination of RNA polymerase II transcription	PMID:19854134^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10531363^[10]	ECO:0000305	curator inference used in manual assertion	GO:0000993	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10899127^[2]	ECO:0000305	curator inference used in manual assertion	GO:0031064 GO:2000749	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10899126^[5]	ECO:0000305	curator inference used in manual assertion	GO:0045944	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14704159^[9]	ECO:0000305	curator inference used in manual assertion	GO:0000122 GO:0006369	C	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:15728580^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:9867817^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:15728580^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:10899126^[5]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	F	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:10531363^[10]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	F	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	PMID:15728580^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	PMID:15728580^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:14704159^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003011 SGD:S000003295 SGD:S000004470	P	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:14704159^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346036 PANTHER:PTN002579701 RGD:1310299 TAIR:locus:2060922	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015379 MGI:MGI:1346036 PANTHER:PTN000069608 PomBase:SPCC16C4.03 RGD:1310299 UniProtKB:Q13526 dictyBase:DDB_G0268618	C	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346036 MGI:MGI:3649546 PANTHER:PTN002579701 SGD:S000003778 TAIR:locus:2060922 UniProtKB:Q13526 dictyBase:DDB_G0268618	F	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000297	F	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.2.1.8	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0697	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Wang, P et al. (2014) Identification and functional analysis of a novel parvulin-type peptidyl-prolyl isomerase from Gossypium hirsutum. Plant Physiol. Biochem. 76 58-66 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Arévalo-Rodríguez, M et al. (2000) Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19 3739-49 PubMed GONUTS page
↑ Siepe, D & Jentsch, S (2009) Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Nat. Cell Biol. 11 967-72 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Ma, Z et al. (2012) Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle. Mol. Cell. Biol. 32 3594-607 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Wu, X et al. (2000) The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19 3727-38 PubMed GONUTS page
↑ Wilcox, CB et al. (2004) Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA Pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae. Genetics 167 93-105 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Singh, N et al. (2009) The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway. Mol. Cell 36 255-66 PubMed GONUTS page
↑ Kops, O et al. (2002) Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1. FEBS Lett. 513 305-11 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Wu, X et al. (2003) The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae. Genetics 165 1687-702 PubMed GONUTS page
↑ ^10.0 ^10.1 Morris, DP et al. (1999) Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation. J. Biol. Chem. 274 31583-7 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Gemmill, TR et al. (2005) Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280 15510-7 PubMed GONUTS page
↑ Hani, J et al. (1999) 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. 274 108-16 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:24468661-1] Wang, P et al. (2014) Identification and functional analysis of a novel parvulin-type peptidyl-prolyl isomerase from Gossypium hirsutum. Plant Physiol. Biochem. 76 58-66 PubMed GONUTS page

[PMID:10899127-2] 2.0 ^2.1 ^2.2 ^2.3 Arévalo-Rodríguez, M et al. (2000) Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19 3739-49 PubMed GONUTS page

[PMID:19597489-3] Siepe, D & Jentsch, S (2009) Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Nat. Cell Biol. 11 967-72 PubMed GONUTS page

[PMID:22778132-4] 4.0 ^4.1 ^4.2 ^4.3 Ma, Z et al. (2012) Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle. Mol. Cell. Biol. 32 3594-607 PubMed GONUTS page

[PMID:10899126-5] 5.0 ^5.1 ^5.2 ^5.3 Wu, X et al. (2000) The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19 3727-38 PubMed GONUTS page

[PMID:15166139-6] Wilcox, CB et al. (2004) Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA Pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae. Genetics 167 93-105 PubMed GONUTS page

[PMID:19854134-7] 7.0 ^7.1 ^7.2 Singh, N et al. (2009) The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway. Mol. Cell 36 255-66 PubMed GONUTS page

[PMID:11904169-8] Kops, O et al. (2002) Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1. FEBS Lett. 513 305-11 PubMed GONUTS page

[PMID:14704159-9] 9.0 ^9.1 ^9.2 ^9.3 Wu, X et al. (2003) The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae. Genetics 165 1687-702 PubMed GONUTS page

[PMID:10531363-10] 10.0 ^10.1 Morris, DP et al. (1999) Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation. J. Biol. Chem. 274 31583-7 PubMed GONUTS page

[PMID:15728580-11] 11.0 ^11.1 ^11.2 ^11.3 Gemmill, TR et al. (2005) Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280 15510-7 PubMed GONUTS page

[PMID:9867817-12] Hani, J et al. (1999) 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. 274 108-16 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:ESS1

Contents

Annotations

Notes

References

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