P20081 (FKBP_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin organization Inferred from genetic interaction Ref.9. Source: SGD protein folding Inferred from mutant phenotype PubMed 9362068. Source: SGD regulation of homoserine biosynthetic process Inferred from genetic interaction PubMed 15470257. Source: SGD
Cellular_component	membrane Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrion Inferred from direct assay PubMed 16823961. Source: SGD nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.3. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD27	P43573	2	EBI-6961,EBI-22787
FAP1	P53971	3	EBI-6961,EBI-28638
HOM3	P10869	5	EBI-6961,EBI-2430
TOR	Q9FR53	3	EBI-6961,EBI-1382370	From a different organism.

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

89

PPIase FKBP-type

Amino acid modifications

Modified residue

46

1

Phosphoserine Ref.13

Modified residue

51

1

Phosphoserine Ref.12 Ref.13

Experimental info

Mutagenesis

43

1

F → Y: Reduces interaction with FAP1. Ref.10

Mutagenesis

44

1

D → V: Abrogates interaction with FAP1. Ref.10

Mutagenesis

48

1

D → V: Abrogates interaction with FAP1. Ref.10

Mutagenesis

49

1

R → I: Abrogates interaction with FAP1. Ref.10

Mutagenesis

94

1

F → V: Abrogates interaction with FAP1. Ref.10

Mutagenesis

106

1

F → Y: Reduces interaction with FAP1. Ref.10

Secondary structure

1

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114

Helix Strand Turn

Details...

Helix

6 – 8

3

Beta strand

10 – 15

6

Beta strand

28 – 37

10

Beta strand

42 – 46

5

Turn

47 – 50

4

Beta strand

53 – 56

4

Beta strand

59 – 62

4

Helix

64 – 69

6

Helix

70 – 72

3

Beta strand

78 – 83

6

Helix

85 – 87

3

Turn

88 – 92

5

Turn

95 – 97

3

Beta strand

104 – 113

10

Sequences

	Sequence		Length	Mass (Da)
	P20081 [UniParc]. Last modified May 1, 1991. Version 2. Checksum: 65C134830D300C06	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

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] [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. , 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 96604 / S288c / FY1679.
[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. , 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY.
[13]	"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-46 AND SER-51, MASS SPECTROMETRY.
[14]	"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.

PIR

A33146. A37870.

RefSeq

NP_014264.1. NM_001182973.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P20081.

SMR

P20081. Positions 2-114.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1263N.

IntAct

P20081. 36 interactions.

MINT

MINT-389324.

STRING

4932.YNL135C.

Proteomic databases

PaxDb

P20081.

PeptideAtlas

P20081.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL135C; YNL135C; YNL135C.

GeneID

855587.

KEGG

sce:YNL135C.

Organism-specific databases

CYGD

YNL135c.

SGD

S000005079. FPR1.

Phylogenomic databases

eggNOG

COG0545.

GeneTree

ENSGT00550000074272.

HOGENOM

HOG000154887.

KO

K09568.

OMA

DGSTYPK.

OrthoDB

EOG4C2MM6.

Gene expression databases

Genevestigator

P20081.

GermOnline

YNL135C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]

PANTHER

PTHR10516. PTHR10516. 1 hit.

Pfam

PF00254. FKBP_C. 1 hit.
[Graphical view]

PROSITE

PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20081.

NextBio

979724.

Entry information

Entry name

FKBP_YEAST

Accession

Primary (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 3, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program