P20081 · FKBP_YEAST

Function

function

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

Miscellaneous

Binds to the immunosuppressant drug FK506 and also mediates the sensitivity to rapamycin (PubMed:1996117).
Rapamycin disrupts interaction with FAP1
Present with 43300 molecules/cell in log phase SD medium.

Catalytic activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular FunctionDNA-binding transcription activator activity, RNA polymerase II-specific
Molecular Functionmacrolide binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionprotein folding chaperone
Biological Processchromatin organization
Biological Processnonfunctional rRNA decay
Biological Processprotein folding
Biological Processregulation of chaperone-mediated protein folding
Biological Processregulation of homoserine biosynthetic process
Biological Processtranscription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    FK506-binding protein 1
  • Short names
    FKBP
  • Alternative names
    • 12-kDa cytosolic FK506-binding protein (FKBP-12)
    • Peptidyl-prolyl cis-trans isomerase (PPIase) (EC:5.2.1.8
      ) . EC:5.2.1.8 (UniProtKB | ENZYME | Rhea)
    • Rapamycin-binding protein

Gene names

    • Name
      FPR1
    • Synonyms
      FKB1, RBP1
    • ORF names
      N1213, N1845
    • Ordered locus names
      YNL135C

Organism names

Accessions

  • Primary accession
    P20081
  • Secondary accessions
    • D6W147

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis43Reduces interaction with FAP1.
Mutagenesis44Abrogates interaction with FAP1.
Mutagenesis48Abrogates interaction with FAP1.
Mutagenesis49Abrogates interaction with FAP1.
Mutagenesis94Abrogates interaction with FAP1.
Mutagenesis106Reduces interaction with FAP1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00000753052-114FK506-binding protein 1
Modified residue51Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with HMO1. Interacts with FAP1.

Binary interactions

Type
Entry 1Entry 2Number of experimentsIntAct
BINARY P20081BUD27 P435732EBI-6961, EBI-22787
BINARY P20081HOM3 P108694EBI-6961, EBI-2430
XENO P20081TOR Q9FR533EBI-6961, EBI-1382370
BINARY P20081TOR1 P351694EBI-6961, EBI-19374
BINARY P20081TOR2 P326003EBI-6961, EBI-19385

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain26-114PPIase FKBP-type

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    114
  • Mass (Da)
    12,158
  • Last updated
    1991-05-01 v2
  • Checksum
    65C134830D300C06
MSEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGSPFQCNIGVGQVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPNSTLVFDVELLKVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z46843
EMBL· GenBank· DDBJ
CAA86890.1
EMBL· GenBank· DDBJ
Genomic DNA
M57967
EMBL· GenBank· DDBJ
AAA03564.1
EMBL· GenBank· DDBJ
Unassigned DNA
M60877
EMBL· GenBank· DDBJ
AAA34607.1
EMBL· GenBank· DDBJ
Genomic DNA
M63892
EMBL· GenBank· DDBJ
AAA34962.1
EMBL· GenBank· DDBJ
mRNA
Z71411
EMBL· GenBank· DDBJ
CAA96017.1
EMBL· GenBank· DDBJ
Genomic DNA
AY557997
EMBL· GenBank· DDBJ
AAS56323.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006947
EMBL· GenBank· DDBJ
DAA10413.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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