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P14832

- CYPH_YEAST

UniProt

P14832 - CYPH_YEAST

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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CPR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

Enzyme regulationi

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

GO - Molecular functioni

  1. cyclosporin A binding Source: SGD
  2. peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  1. ascospore formation Source: SGD
  2. cellular protein metabolic process Source: SGD
  3. histone deacetylation Source: SGD
  4. positive regulation of meiosis Source: SGD
  5. protein folding Source: UniProtKB-KW
  6. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciYEAST:YDR155C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Short name:
CPH
Cyclosporin A-binding protein
PPI-II
Rotamase
Gene namesi
Name:CPR1
Synonyms:CPH1, CYP1, SCC1
Ordered Locus Names:YDR155C
ORF Names:YD8358.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002562. CPR1.

Subcellular locationi

GO - Cellular componenti

  1. histone deacetylase complex Source: SGD
  2. mitochondrial intermembrane space Source: SGD
  3. nucleus Source: SGD
  4. Set3 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 162161Peptidyl-prolyl cis-trans isomerasePRO_0000064132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei71 – 711Phosphothreonine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei145 – 1451Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14832.
PaxDbiP14832.
PeptideAtlasiP14832.
PRIDEiP14832.

Expressioni

Gene expression databases

GenevestigatoriP14832.

Interactioni

Subunit structurei

Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3.3 Publications

Protein-protein interaction databases

BioGridi32207. 84 interactions.
DIPiDIP-5203N.
IntActiP14832. 63 interactions.
MINTiMINT-494205.
STRINGi4932.YDR155C.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi13 – 2210
Turni24 – 263
Helixi28 – 3912
Turni40 – 423
Beta strandi53 – 553
Turni56 – 583
Beta strandi59 – 624
Turni65 – 673
Beta strandi68 – 714
Beta strandi92 – 987
Beta strandi100 – 1023
Beta strandi110 – 1156
Helixi118 – 1203
Turni121 – 1233
Beta strandi126 – 1327
Helixi134 – 1418
Beta strandi154 – 1618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISTX-ray1.90A/B1-162[»]
1VDNX-ray1.60A1-162[»]
ProteinModelPortaliP14832.
SMRiP14832. Positions 2-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 161157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP14832.
KOiK01802.
OMAiFRELCTH.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14832-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP
60 70 80 90 100
FHRVIPDFML QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN
110 120 130 140 150
AGPNTNGSQF FITTVPCPWL DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT
160
KARIVVAKSG EL
Length:162
Mass (Da):17,391
Last modified:January 23, 2007 - v3
Checksum:i012D8E8E4D85B4B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS25443. CSBY.
RefSeqiNP_010439.1. NM_001180462.1.

Genome annotation databases

EnsemblFungiiYDR155C; YDR155C; YDR155C.
GeneIDi851733.
KEGGisce:YDR155C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S25443. CSBY.
RefSeqi NP_010439.1. NM_001180462.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IST X-ray 1.90 A/B 1-162 [» ]
1VDN X-ray 1.60 A 1-162 [» ]
ProteinModelPortali P14832.
SMRi P14832. Positions 2-162.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32207. 84 interactions.
DIPi DIP-5203N.
IntActi P14832. 63 interactions.
MINTi MINT-494205.
STRINGi 4932.YDR155C.

Proteomic databases

MaxQBi P14832.
PaxDbi P14832.
PeptideAtlasi P14832.
PRIDEi P14832.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR155C ; YDR155C ; YDR155C .
GeneIDi 851733.
KEGGi sce:YDR155C.

Organism-specific databases

SGDi S000002562. CPR1.

Phylogenomic databases

eggNOGi COG0652.
GeneTreei ENSGT00760000119119.
HOGENOMi HOG000065981.
InParanoidi P14832.
KOi K01802.
OMAi FRELCTH.
OrthoDBi EOG757D7G.

Enzyme and pathway databases

BioCyci YEAST:YDR155C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P14832.
NextBioi 969457.

Gene expression databases

Genevestigatori P14832.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. 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. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. 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).

Entry informationi

Entry nameiCYPH_YEAST
AccessioniPrimary (citable) accession number: P14832
Secondary accession number(s): D6VSD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
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 86000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3