Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14832 (CYPH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin
Short name=CPH
Cyclosporin A-binding protein
PPI-II
Rotamase
Gene names
Name:CPR1
Synonyms:CPH1, CYP1, SCC1
Ordered Locus Names:YDR155C
ORF Names:YD8358.10C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function. Ref.6 Ref.10 Ref.11

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). Ref.6

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

Subunit structure

Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3. Ref.7 Ref.8 Ref.11

Subcellular location

Cytoplasm. Nucleus. Mitochondrion intermembrane space Ref.11 Ref.16.

Miscellaneous

Present with 86000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.6
Chain2 – 162161Peptidyl-prolyl cis-trans isomerase
PRO_0000064132

Regions

Domain5 – 161157PPIase cyclophilin-type

Amino acid modifications

Modified residue21N-acetylserine Ref.2 Ref.6 Ref.17
Modified residue711Phosphothreonine Ref.14
Modified residue1421Phosphoserine Ref.14
Modified residue1451Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15

Secondary structure

................................ 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14832 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 012D8E8E4D85B4B7

FASTA16217,391
        10         20         30         40         50         60 
MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP FHRVIPDFML 

        70         80         90        100        110        120 
QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN AGPNTNGSQF FITTVPCPWL 

       130        140        150        160 
DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT KARIVVAKSG EL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a full-length cDNA coding for cyclophilin (peptidyl-prolyl cis-trans isomerase) of Saccharomyces cerevisiae."
Dietmeier K., Tropschug M.
Nucleic Acids Res. 18:373-373(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene."
Haendler B., Keller R., Hiestand P.C., Kocher H.P., Wegmann G., Movva N.R.
Gene 83:39-46(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-112 AND 120-151, ACETYLATION AT SER-2, CLEAVAGE OF INITIATOR METHIONINE.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Purification and properties of multiple molecular forms of yeast peptidyl prolyl cis-trans isomerase."
Hasumi H., Nishikawa T.
Biochim. Biophys. Acta 1161:161-167(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 2-10; 30-37; 75-78; 81-85 AND 159-162, FUNCTION, CATALYTIC ACTIVITY.
[7]"The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program."
Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.
Genes Dev. 15:2991-3004(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; YIL112W AND SET3.
[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 RPD3.
[9]"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].
[10]"Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles."
Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L.
J. Biol. Chem. 276:48017-48026(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae."
Arevalo-Rodriguez M., Heitman J.
Eukaryot. Cell 4:17-29(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET3C COMPLEX, INTERACTION WITH SNT1 AND SIF2.
[12]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[13]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 THR-71; SER-142 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Intermembrane space proteome of yeast mitochondria."
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.
Mol. Cell. Proteomics 11:1840-1852(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Turns are essential in the folding of the globular beta-barrel structure of yeast cyclophilin A, CPR1."
Kashima A., Yoshikawa-Fujioka S., Hayano T., Takahashi N., Konno M.
Submitted (DEC-2001) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
[20]"Crystal structure of yeast cyclophilin A complexed with ACE-Ala-Ala-Pro-Ala-7-amino-4-methylcoumarin."
Konno M., Shibano T., Okudaira K., Takahashi N.
Submitted (MAR-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17505 mRNA. Translation: CAA35545.1.
M30513 Genomic DNA. Translation: AAA34528.1.
Z50046 Genomic DNA. Translation: CAA90376.1.
AY557665 Genomic DNA. Translation: AAS55991.1.
BK006938 Genomic DNA. Translation: DAA11996.1.
PIRCSBY. S25443.
RefSeqNP_010439.1. NM_001180462.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISTX-ray1.90A/B1-162[»]
1VDNX-ray1.60A1-162[»]
ProteinModelPortalP14832.
SMRP14832. Positions 2-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32207. 83 interactions.
DIPDIP-5203N.
IntActP14832. 63 interactions.
MINTMINT-494205.
STRING4932.YDR155C.

Proteomic databases

MaxQBP14832.
PaxDbP14832.
PeptideAtlasP14832.
PRIDEP14832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR155C; YDR155C; YDR155C.
GeneID851733.
KEGGsce:YDR155C.

Organism-specific databases

SGDS000002562. CPR1.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00750000117619.
HOGENOMHOG000065981.
KOK01802.
OMAFRELCTH.
OrthoDBEOG757D7G.

Enzyme and pathway databases

BioCycYEAST:YDR155C-MONOMER.

Gene expression databases

GenevestigatorP14832.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14832.
NextBio969457.

Entry information

Entry nameCYPH_YEAST
AccessionPrimary (citable) accession number: P14832
Secondary accession number(s): D6VSD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references