UniProt Accession

 ESS1_YEAST; P22696; D6VWJ3 

Genbank Protein ID

 X85972; X87611; Z49517; BK006943 

Genbank Nucleotide ID

 CAA59961.1; CAA60941.1; CAA89541.1; DAA08809.1 

Protein Name

 Peptidyl-prolyl cis-trans isomerase ESS1 

Protein Synonyms/Alias

 PPIase ESS1; Parvulin ESS1; Processing/termination factor 1 

Gene Name

 ESS1 

Gene Synonyms/Alias

 PIN1; PTF1; YJR017C; J1452 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
46	EEPEGTNKDQLHKHL	acetylation	[1]
106	TRLDDDSKTNSFEAL	acetylation	[1]
106	TRLDDDSKTNSFEAL	ubiquitination	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 

Functional Description

 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). 

Sequence Annotation

 DOMAIN 9 43 WW.
 DOMAIN 57 170 PpiC.
 MOD_RES 161 161 Phosphoserine.  

Keyword

 Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein; Reference proteome; Rotamase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 170 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IC:SGD.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
 GO:0031064; P:negative regulation of histone deacetylation; IMP:SGD.
 GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:SGD.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
 GO:2000749; P:positive regulation of chromatin silencing at rDNA; IMP:SGD.
 GO:0035307; P:positive regulation of protein dephosphorylation; IDA:SGD.
 GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IGI:SGD.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0000114; P:regulation of transcription involved in G1 phase of mitotic cell cycle; IMP:SGD.
 GO:0000117; P:regulation of transcription involved in G2/M-phase of mitotic cell cycle; IMP:SGD.
 GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD. 

Interpro

 IPR000297; PPIase_PpiC.
 IPR023058; PPIase_PpiC_CS.
 IPR001202; WW_dom. 

Pfam

 PF00639; Rotamase
 PF00397; WW 

SMART

 SM00456; WW 

PROSITE

 PS01096; PPIC_PPIASE_1
 PS50198; PPIC_PPIASE_2
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 

PRINTS