Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20081 (FKBP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.9 Ref.10

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.

Sequence similarities

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

Contains 1 PPIase FKBP-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUD27P435732EBI-6961,EBI-22787
TORQ9FR533EBI-6961,EBI-1382370From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 114113FK506-binding protein 1
PRO_0000075305

Regions

Domain26 – 11489PPIase FKBP-type

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue511Phosphoserine Ref.12 Ref.13

Experimental info

Mutagenesis431F → Y: Reduces interaction with FAP1. Ref.10
Mutagenesis441D → V: Abrogates interaction with FAP1. Ref.10
Mutagenesis481D → V: Abrogates interaction with FAP1. Ref.10
Mutagenesis491R → I: Abrogates interaction with FAP1. Ref.10
Mutagenesis941F → V: Abrogates interaction with FAP1. Ref.10
Mutagenesis1061F → Y: Reduces interaction with FAP1. Ref.10

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P20081 [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] [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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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).
+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.
BK006947 Genomic DNA. Translation: DAA10413.1.
PIRA33146. A37870.
RefSeqNP_014264.1. NM_001182973.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YATX-ray2.50A2-114[»]
ProteinModelPortalP20081.
SMRP20081. Positions 2-114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35691. 132 interactions.
DIPDIP-1263N.
IntActP20081. 20 interactions.
MINTMINT-389324.
STRING4932.YNL135C.

Proteomic databases

PaxDbP20081.
PeptideAtlasP20081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL135C; YNL135C; YNL135C.
GeneID855587.
KEGGsce:YNL135C.

Organism-specific databases

CYGDYNL135c.
SGDS000005079. FPR1.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00550000074272.
HOGENOMHOG000154887.
KOK09568.
OMAFQCNIGV.
OrthoDBEOG77WWQ3.

Enzyme and pathway databases

BioCycYEAST:YNL135C-MONOMER.

Gene expression databases

GenevestigatorP20081.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20081.
NextBio979724.
PROP20081.

Entry information

Entry nameFKBP_YEAST
AccessionPrimary (citable) accession number: P20081
Secondary accession number(s): D6W147
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references