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P38911

- FKBP3_YEAST

UniProt

P38911 - FKBP3_YEAST

Protein

FK506-binding nuclear protein

Gene

FPR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. FK506- and rapamycin-binding protein. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by both FK506 and rapamycin.

    GO - Molecular functioni

    1. FK506 binding Source: InterPro
    2. macrolide binding Source: SGD
    3. peptidyl-prolyl cis-trans isomerase activity Source: SGD

    GO - Biological processi

    1. histone peptidyl-prolyl isomerization Source: InterPro
    2. meiotic recombination checkpoint Source: SGD
    3. nucleosome assembly Source: SGD
    4. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciYEAST:YML074C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FK506-binding nuclear protein (EC:5.2.1.8)
    Alternative name(s):
    FKBP-70
    Nucleolar proline isomerase
    Peptidyl-prolyl cis-trans isomerase
    Short name:
    PPIase
    Proline rotamase
    Gene namesi
    Name:FPR3
    Synonyms:NPI46
    Ordered Locus Names:YML074C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML074c.
    SGDiS000004539. FPR3.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 411410FK506-binding nuclear proteinPRO_0000075313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei80 – 801Phosphoserine3 Publications
    Modified residuei81 – 811Phosphoserine3 Publications
    Modified residuei89 – 891Phosphothreonine1 Publication
    Modified residuei184 – 1841Phosphotyrosine; by CK21 Publication
    Modified residuei186 – 1861Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Phosphorylated at tyrosine and dephosphorylated by the phosphotyrosine-specific phosphoprotein phosphatase PTP1.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP38911.
    PaxDbiP38911.
    PeptideAtlasiP38911.

    Expressioni

    Gene expression databases

    GenevestigatoriP38911.

    Interactioni

    Subunit structurei

    Interacts with NOP53.1 Publication

    Protein-protein interaction databases

    BioGridi35067. 71 interactions.
    DIPiDIP-6578N.
    IntActiP38911. 59 interactions.
    MINTiMINT-673400.
    STRINGi4932.YML074C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38911.
    SMRiP38911. Positions 266-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini324 – 41188PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi256 – 27116Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 8728Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi88 – 9912Lys-rich (highly basic)Add
    BLAST
    Compositional biasi101 – 11919Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi173 – 24876Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi250 – 29849Lys-rich (highly basic)Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00530000064286.
    HOGENOMiHOG000216214.
    KOiK14826.
    OMAiKGECIKG.
    OrthoDBiEOG77WWQ3.

    Family and domain databases

    InterProiIPR026257. FK506_BP.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001473. FK506-bp_FPR3. 1 hit.
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P38911-1 [UniParc]FASTAAdd to Basket

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    MSDLLPLATY SLNVEPYTPV PAIDVTMPIT VRITMAALNP EAIDEENKPS    50
    TLRIIKRNPD FEDDDFLGGD FDEDEIDEES SEEEEEEKTQ KKKKSKGKKA 100
    ESESEDDEED DDEDDEFQES VLLTLSPEAQ YQQSLDLTIT PEEEVQFIVT 150
    GSYAISLSGN YVKHPFDTPM GVEGEDEDED ADIYDSEDYD LTPDEDEIIG 200
    DDMDDLDDEE EEEVRIEEVQ EEDEEDNDGE EEQEEEEEEE QKEEVKPEPK 250
    KSKKEKKRKH EEKEEEKKAK KVKKVEFKKD LEEGPTKPKS KKEQDKHKPK 300
    SKVLEGGIVI EDRTIGDGPQ AKRGARVGMR YIGKLKNGKV FDKNTSGKPF 350
    AFKLGRGEVI KGWDIGVAGM SVGGERRIII PAPYAYGKQA LPGIPANSEL 400
    TFDVKLVSMK N 411
    Length:411
    Mass (Da):46,553
    Last modified:November 1, 1995 - v2
    Checksum:iA01D24DE0078FE11
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221L → P in AAB04165. (PubMed:7925954)Curated
    Sequence conflicti240 – 2401E → EEE(PubMed:7925954)Curated
    Sequence conflicti335 – 3351L → F in AAB04165. (PubMed:7925954)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34569 Genomic DNA. Translation: AAB04165.1.
    X79379 Genomic DNA. Translation: CAA55924.1.
    S73876 Genomic DNA. Translation: AAB31995.1.
    Z46373 Genomic DNA. Translation: CAA86504.1.
    AY693136 Genomic DNA. Translation: AAT93155.1.
    BK006946 Genomic DNA. Translation: DAA09823.1.
    PIRiS48647.
    RefSeqiNP_013637.1. NM_001182433.1.

    Genome annotation databases

    EnsemblFungiiYML074C; YML074C; YML074C.
    GeneIDi854901.
    KEGGisce:YML074C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34569 Genomic DNA. Translation: AAB04165.1 .
    X79379 Genomic DNA. Translation: CAA55924.1 .
    S73876 Genomic DNA. Translation: AAB31995.1 .
    Z46373 Genomic DNA. Translation: CAA86504.1 .
    AY693136 Genomic DNA. Translation: AAT93155.1 .
    BK006946 Genomic DNA. Translation: DAA09823.1 .
    PIRi S48647.
    RefSeqi NP_013637.1. NM_001182433.1.

    3D structure databases

    ProteinModelPortali P38911.
    SMRi P38911. Positions 266-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35067. 71 interactions.
    DIPi DIP-6578N.
    IntActi P38911. 59 interactions.
    MINTi MINT-673400.
    STRINGi 4932.YML074C.

    Proteomic databases

    MaxQBi P38911.
    PaxDbi P38911.
    PeptideAtlasi P38911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML074C ; YML074C ; YML074C .
    GeneIDi 854901.
    KEGGi sce:YML074C.

    Organism-specific databases

    CYGDi YML074c.
    SGDi S000004539. FPR3.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00530000064286.
    HOGENOMi HOG000216214.
    KOi K14826.
    OMAi KGECIKG.
    OrthoDBi EOG77WWQ3.

    Enzyme and pathway databases

    BioCyci YEAST:YML074C-MONOMER.

    Miscellaneous databases

    NextBioi 977879.

    Gene expression databases

    Genevestigatori P38911.

    Family and domain databases

    InterProi IPR026257. FK506_BP.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001473. FK506-bp_FPR3. 1 hit.
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification of FKBP-70, a novel immunophilin from Saccharomyces cerevisiae, and cloning of its structural gene, FPR3."
      Manning-Krieg U.C., Henriquez R., Cammas F., Graff P., Gaveriaux S., Movva N.R.
      FEBS Lett. 352:98-103(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus."
      Shan X., Xue Z., Melese T.
      J. Cell Biol. 126:853-862(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus."
      Benton B.M., Zang J.-H., Thorner J.
      J. Cell Biol. 127:623-639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: YNN 214.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3."
      Wilson L.K., Dhillon N., Thorner J., Martin G.S.
      J. Biol. Chem. 272:12961-12967(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-184 AND SER-186.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein."
      Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D.
      Biochem. J. 388:819-826(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOP53, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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-80 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "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-80 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-80; SER-81 AND THR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFKBP3_YEAST
    AccessioniPrimary (citable) accession number: P38911
    Secondary accession number(s): D6W0K9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 9490 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3