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Reviewed, UniProtKB/Swiss-Prot P20081 (FKBP_YEAST)

Last modified January 19, 2010. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    FK506-binding protein 1
      Short name=FKBP
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
    EC=5.2.1.8
    Rapamycin-binding protein
Gene names
Name: FPR1
Synonyms: FKB1, RBP1
Ordered Locus Names: YNL135C
ORF Names: N1213, N1845
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
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.

Catalytic activity

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

Subunit structure

Interacts with HMO1. Interacts with FAP1. Ref.8 Ref.9

Subcellular location

Cytoplasm.

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. Ref.10

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUD27P435731EBI-6961,EBI-22787
FAP1P539711EBI-6961,EBI-28638
HOM3P108693EBI-6961,EBI-2430
TORQ9FR533EBI-6961,EBI-1382370From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114FK506-binding protein 1
PRO_0000075305

Regions

Domain26 – 11489PPIase FKBP-type

Amino acid modifications

Modified residue461Phosphoserine Ref.12
Modified residue511Phosphoserine Ref.12 Ref.11

Experimental info

Mutagenesis431F → Y: Reduces interaction with FAP1. Ref.9
Mutagenesis441D → V: Abrogates interaction with FAP1. Ref.9
Mutagenesis481D → V: Abrogates interaction with FAP1. Ref.9
Mutagenesis491R → I: Abrogates interaction with FAP1. Ref.9
Mutagenesis941F → V: Abrogates interaction with FAP1. Ref.9
Mutagenesis1061F → Y: Reduces interaction with FAP1. Ref.9

Secondary structure

.......................... 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20081-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 65C134830D300C06

FASTA11412,158
        10         20         30         40         50         60 
MSEVIEGNVK IDRISPGDGA TFPKTGDLVT IHYTGTLENG QKFDSSVDRG SPFQCNIGVG 

        70         80         90        100        110 
QVIKGWDVGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP NSTLVFDVEL LKVN 

« Hide

References

« Hide 'large scale' references
[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: 1704127] [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: 1705713] [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: 1996117] [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: 8619318] [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. expand/collapse author list , 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: 9169873] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[6]"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: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"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: 1701173] [Abstract]
Cited for: PROTEIN SEQUENCE OF 67-100.
[8]"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: 10049913] [Abstract]
Cited for: INTERACTION WITH HMO1.
[9]"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: 10998178] [Abstract]
Cited for: INTERACTION WITH FAP1, MUTAGENESIS OF PHE-43; ASP-44; ASP-48; ARG-49; PHE-94 AND PHE-106.
[10]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-51, MASS SPECTROMETRY.
[13]"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: 7681823] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA33146. A37870.
RefSeqNP_014264.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YATX-ray2.50A2-114[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1263N.
IntActP20081. 37 interactions.
STRINGP20081.

Proteomic databases

PeptideAtlasP20081.
PRIDEP20081.

Genome annotation databases

EnsemblYNL135C; YNL135C; YNL135C; Saccharomyces cerevisiae. [Genome view]
GeneID855587.
KEGGsce:YNL135C.
NMPDRfig|4932.3.peg.5333.

Organism-specific databases

CYGDYNL135c.
SGDS000005079. FPR1.

Phylogenomic databases

eggNOGfuNOG09243.
HOGENOMHBG731200.
OMASVDRGSP.
OrthoDBEOG9PNZZZ.
PhylomeDBP20081.

Enzyme and pathway databases

BRENDA5.2.1.8. 250.

Gene expression databases

ArrayExpressP20081.
GenevestigatorP20081.
GermOnlineYNL135C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio979724.

Entry information

Entry nameFKBP_YEAST
AccessionPrimary (citable) accession number: P20081
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 1991
Last modified: January 19, 2010
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIV

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents