Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20081

- FKBP_YEAST

UniProt

P20081 - FKBP_YEAST

Protein

FK506-binding protein 1

Gene

FPR1

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

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    Catalytic activityi

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

    GO - Molecular functioni

    1. macrolide binding Source: SGD
    2. peptidyl-prolyl cis-trans isomerase activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin organization Source: SGD
    2. protein folding Source: SGD
    3. protein peptidyl-prolyl isomerization Source: GOC
    4. regulation of homoserine biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciYEAST:YNL135C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FK506-binding protein 1
    Short name:
    FKBP
    Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
    Short name:
    PPIase
    Rapamycin-binding protein
    Gene namesi
    Name:FPR1
    Synonyms:FKB1, RBP1
    Ordered Locus Names:YNL135C
    ORF Names:N1213, N1845
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL135c.
    SGDiS000005079. FPR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431F → Y: Reduces interaction with FAP1. 1 Publication
    Mutagenesisi44 – 441D → V: Abrogates interaction with FAP1. 1 Publication
    Mutagenesisi48 – 481D → V: Abrogates interaction with FAP1. 1 Publication
    Mutagenesisi49 – 491R → I: Abrogates interaction with FAP1. 1 Publication
    Mutagenesisi94 – 941F → V: Abrogates interaction with FAP1. 1 Publication
    Mutagenesisi106 – 1061F → Y: Reduces interaction with FAP1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 114113FK506-binding protein 1PRO_0000075305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei51 – 511Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP20081.
    PaxDbiP20081.
    PeptideAtlasiP20081.

    Expressioni

    Gene expression databases

    GenevestigatoriP20081.

    Interactioni

    Subunit structurei

    Interacts with HMO1. Interacts with FAP1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUD27P435732EBI-6961,EBI-22787
    TORQ9FR533EBI-6961,EBI-1382370From a different organism.

    Protein-protein interaction databases

    BioGridi35691. 132 interactions.
    DIPiDIP-1263N.
    IntActiP20081. 20 interactions.
    MINTiMINT-389324.
    STRINGi4932.YNL135C.

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi10 – 156
    Beta strandi28 – 3710
    Beta strandi42 – 465
    Turni47 – 504
    Beta strandi53 – 564
    Beta strandi59 – 624
    Helixi64 – 696
    Helixi70 – 723
    Beta strandi78 – 836
    Helixi85 – 873
    Turni88 – 925
    Turni95 – 973
    Beta strandi104 – 11310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YATX-ray2.50A2-114[»]
    ProteinModelPortaliP20081.
    SMRiP20081. Positions 2-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20081.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 11489PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00550000074272.
    HOGENOMiHOG000154887.
    KOiK09568.
    OMAiSPQKGDT.
    OrthoDBiEOG77WWQ3.

    Family and domain databases

    InterProiIPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20081-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEVIEGNVK IDRISPGDGA TFPKTGDLVT IHYTGTLENG QKFDSSVDRG    50
    SPFQCNIGVG QVIKGWDVGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP 100
    NSTLVFDVEL LKVN 114
    Length:114
    Mass (Da):12,158
    Last modified:May 1, 1991 - v2
    Checksum:i65C134830D300C06
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46843 Genomic DNA. Translation: CAA86890.1.
    M57967 Unassigned DNA. Translation: AAA03564.1.
    M60877 Genomic DNA. Translation: AAA34607.1.
    M63892 mRNA. Translation: AAA34962.1.
    Z71411 Genomic DNA. Translation: CAA96017.1.
    AY557997 Genomic DNA. Translation: AAS56323.1.
    BK006947 Genomic DNA. Translation: DAA10413.1.
    PIRiA37870. A33146.
    RefSeqiNP_014264.1. NM_001182973.1.

    Genome annotation databases

    EnsemblFungiiYNL135C; YNL135C; YNL135C.
    GeneIDi855587.
    KEGGisce:YNL135C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46843 Genomic DNA. Translation: CAA86890.1 .
    M57967 Unassigned DNA. Translation: AAA03564.1 .
    M60877 Genomic DNA. Translation: AAA34607.1 .
    M63892 mRNA. Translation: AAA34962.1 .
    Z71411 Genomic DNA. Translation: CAA96017.1 .
    AY557997 Genomic DNA. Translation: AAS56323.1 .
    BK006947 Genomic DNA. Translation: DAA10413.1 .
    PIRi A37870. A33146.
    RefSeqi NP_014264.1. NM_001182973.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YAT X-ray 2.50 A 2-114 [» ]
    ProteinModelPortali P20081.
    SMRi P20081. Positions 2-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35691. 132 interactions.
    DIPi DIP-1263N.
    IntActi P20081. 20 interactions.
    MINTi MINT-389324.
    STRINGi 4932.YNL135C.

    Proteomic databases

    MaxQBi P20081.
    PaxDbi P20081.
    PeptideAtlasi P20081.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL135C ; YNL135C ; YNL135C .
    GeneIDi 855587.
    KEGGi sce:YNL135C.

    Organism-specific databases

    CYGDi YNL135c.
    SGDi S000005079. FPR1.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00550000074272.
    HOGENOMi HOG000154887.
    KOi K09568.
    OMAi SPQKGDT.
    OrthoDBi EOG77WWQ3.

    Enzyme and pathway databases

    BioCyci YEAST:YNL135C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P20081.
    NextBioi 979724.
    PROi P20081.

    Gene expression databases

    Genevestigatori P20081.

    Family and domain databases

    InterProi IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins."
      Wiederrecht G.J., Brizuela L., Elliston K.O., Sigal N.H., Siekierka J.J.
      Proc. Natl. Acad. Sci. U.S.A. 88:1029-1033(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae."
      Heitman J., Movva R.N., Hiestand P.C., Hall M.N.
      Proc. Natl. Acad. Sci. U.S.A. 88:1948-1952(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein."
      Koltin Y., Faucette L., Bergsma D.J., Levy M.A., Cafferkey R., Koser P.L., Johnson R.K., Livi G.P.
      Mol. Cell. Biol. 11:1718-1723(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames."
      Mallet L., Bussereau F., Jacquet M.
      Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    8. "The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase."
      Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., Cryan J., Hodges P.J., Sigal N.H.
      J. Biol. Chem. 265:21011-21015(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 67-100.
    9. "Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase."
      Dolinski K.J., Heitman J.
      Genetics 151:935-944(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HMO1.
    10. "FAP1, a homologue of human transcription factor NF-X1, competes with rapamycin for binding to FKBP12 in yeast."
      Kunz J., Loeschmann A., Deuter-Reinhard M., Hall M.N.
      Mol. Microbiol. 37:1480-1493(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAP1, MUTAGENESIS OF PHE-43; ASP-44; ASP-48; ARG-49; PHE-94 AND PHE-106.
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis."
      Rotonda J., Burbaum J.J., Chan H.K., Marcy A.I., Becker J.W.
      J. Biol. Chem. 268:7607-7609(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiFKBP_YEAST
    AccessioniPrimary (citable) accession number: P20081
    Secondary accession number(s): D6W147
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds to the immunosuppressant drug FK506 and also mediates the sensitivity to rapamycin. Rapamycin disrupts interaction with FAP1.
    Present with 43300 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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3