FK506-binding protein 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P20081 (FKBP_YEAST)

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

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

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Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chromatin organization Ref.8 Inferred from genetic interaction. Source: SGD homoserine metabolic process Inferred from genetic interaction. Source: SGD protein folding Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	macrolide binding Inferred from direct assay. Source: SGD peptidyl-prolyl cis-trans isomerase activity Ref.3 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD27	P43573	1	EBI-6961,EBI-22787
FAP1	P53971	1	EBI-6961,EBI-28638
HOM3	P10869	3	EBI-6961,EBI-2430
TOR	Q9FR53	3	EBI-6961,EBI-1382370	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 114

114

FK506-binding protein 1

PRO_0000075305

Regions

Domain

26 – 114

PPIase FKBP-type

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12 Ref.11

Experimental info

Mutagenesis

F → Y: Reduces interaction with FAP1. Ref.9

Mutagenesis

D → V: Abrogates interaction with FAP1. Ref.9

Mutagenesis

D → V: Abrogates interaction with FAP1. Ref.9

Mutagenesis

R → I: Abrogates interaction with FAP1. Ref.9

Mutagenesis

F → V: Abrogates interaction with FAP1. Ref.9

Mutagenesis

106

F → Y: Reduces interaction with FAP1. Ref.9

Secondary structure

114

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P20081-1 [UniParc].

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

114

12,158

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

        70         80         90        100        110 
QVIKGWDVGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP NSTLVFDVEL LKVN

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References

	« Hide 'large scale' referencesShow '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. 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. 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.

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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.

PIR

A33146. A37870.

RefSeq

NP_014264.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YAT	X-ray	2.50	A	2-114	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1263N.

IntAct

P20081. 37 interactions.

STRING

P20081.

Proteomic databases

PeptideAtlas

P20081.

PRIDE

P20081.

Genome annotation databases

Ensembl

YNL135C; YNL135C; YNL135C; Saccharomyces cerevisiae. [Genome view]

GeneID

855587.

KEGG

sce:YNL135C.

NMPDR

fig|4932.3.peg.5333.

Organism-specific databases

CYGD

YNL135c.

SGD

S000005079. FPR1.

Phylogenomic databases

eggNOG

HOGENOM

OMA

OrthoDB

PhylomeDB

P20081.

Enzyme and pathway databases

BRENDA

5.2.1.8. 250.

Gene expression databases

ArrayExpress

P20081.

Genevestigator

P20081.

GermOnline

YNL135C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001179. PPIase_FKBP.
[Graphical view]

PANTHER

PTHR10516. PPIase_FKBP. 1 hit.

Pfam

PF00254. FKBP_C. 1 hit.
[Graphical view]

PROSITE

PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

979724.

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Entry information

Entry name

FKBP_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents