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Protein

FK506-binding protein 1

Gene

FPR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

  • FK506 binding Source: GO_Central
  • macrolide binding Source: SGD
  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  • chaperone-mediated protein folding Source: GO_Central
  • chromatin organization Source: SGD
  • protein folding Source: SGD
  • regulation of homoserine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YNL135C-MONOMER.
ReactomeiR-SCE-3371568. Attenuation phase.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL135C.
SGDiS000005079. FPR1.

Subcellular locationi

GO - Cellular componenti

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 methionineiRemovedCombined sources
Chaini2 – 114113FK506-binding protein 1PRO_0000075305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei51 – 511PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20081.
TopDownProteomicsiP20081.

PTM databases

iPTMnetiP20081.

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. 138 interactions.
DIPiDIP-1263N.
IntActiP20081. 21 interactions.
MINTiMINT-389324.

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi10 – 156Combined sources
Beta strandi28 – 3710Combined sources
Beta strandi42 – 465Combined sources
Turni47 – 504Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 696Combined sources
Helixi70 – 723Combined sources
Beta strandi78 – 836Combined sources
Helixi85 – 873Combined sources
Turni88 – 925Combined sources
Turni95 – 973Combined sources
Beta strandi104 – 11310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YATX-ray2.50A2-114[»]
ProteinModelPortaliP20081.
SMRiP20081. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20081.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 11489PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
InParanoidiP20081.
KOiK09568.
OMAiVPCWTEG.
OrthoDBiEOG092C52SD.

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

        10         20         30         40         50
MSEVIEGNVK IDRISPGDGA TFPKTGDLVT IHYTGTLENG QKFDSSVDRG
60 70 80 90 100
SPFQCNIGVG QVIKGWDVGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP
110
NSTLVFDVEL LKVN
Length:114
Mass (Da):12,158
Last modified:May 1, 1991 - v2
Checksum:i65C134830D300C06
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YATX-ray2.50A2-114[»]
ProteinModelPortaliP20081.
SMRiP20081. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35691. 138 interactions.
DIPiDIP-1263N.
IntActiP20081. 21 interactions.
MINTiMINT-389324.

PTM databases

iPTMnetiP20081.

Proteomic databases

MaxQBiP20081.
TopDownProteomicsiP20081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL135C; YNL135C; YNL135C.
GeneIDi855587.
KEGGisce:YNL135C.

Organism-specific databases

EuPathDBiFungiDB:YNL135C.
SGDiS000005079. FPR1.

Phylogenomic databases

GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
InParanoidiP20081.
KOiK09568.
OMAiVPCWTEG.
OrthoDBiEOG092C52SD.

Enzyme and pathway databases

BioCyciYEAST:YNL135C-MONOMER.
ReactomeiR-SCE-3371568. Attenuation phase.

Miscellaneous databases

EvolutionaryTraceiP20081.
PROiP20081.

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]
ProtoNetiSearch...

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: September 7, 2016
This is version 163 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.