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P20081

- FKBP_YEAST

UniProt

P20081 - FKBP_YEAST

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Protein

FK506-binding protein 1

Gene
FPR1, FKB1, RBP1, YNL135C, N1213, N1845
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.

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
Complete GO annotation...

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
Complete GO annotation...

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.

Miscellaneous databases

EvolutionaryTraceiP20081.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 11489PPIase FKBP-typeAdd
BLAST

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 142 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.

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

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