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P38911 (FKBP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FK506-binding nuclear protein

EC=5.2.1.8
Alternative name(s):
FKBP-70
Nucleolar proline isomerase
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Proline rotamase
Gene names
Name:FPR3
Synonyms:NPI46
Ordered Locus Names:YML074C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length411 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. FK506- and rapamycin-binding protein. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Interacts with NOP53. Ref.9

Subcellular location

Nucleusnucleolus.

Post-translational modification

Phosphorylated at tyrosine and dephosphorylated by the phosphotyrosine-specific phosphoprotein phosphatase PTP1. Ref.7

Miscellaneous

Present with 9490 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.

Contains 1 PPIase FKBP-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 411410FK506-binding nuclear protein
PRO_0000075313

Regions

Domain324 – 41188PPIase FKBP-type
Motif256 – 27116Nuclear localization signal Potential
Compositional bias60 – 8728Asp/Glu-rich (highly acidic)
Compositional bias88 – 9912Lys-rich (highly basic)
Compositional bias101 – 11919Asp/Glu-rich (highly acidic)
Compositional bias173 – 24876Asp/Glu-rich (highly acidic)
Compositional bias250 – 29849Lys-rich (highly basic)

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue801Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue811Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue891Phosphothreonine Ref.12
Modified residue1841Phosphotyrosine; by CK2 Ref.7
Modified residue1861Phosphoserine; by CK2 Ref.7

Experimental info

Sequence conflict1221L → P in AAB04165. Ref.1
Sequence conflict2401E → EEE Ref.1
Sequence conflict3351L → F in AAB04165. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38911 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: A01D24DE0078FE11

FASTA41146,553
        10         20         30         40         50         60 
MSDLLPLATY SLNVEPYTPV PAIDVTMPIT VRITMAALNP EAIDEENKPS TLRIIKRNPD 

        70         80         90        100        110        120 
FEDDDFLGGD FDEDEIDEES SEEEEEEKTQ KKKKSKGKKA ESESEDDEED DDEDDEFQES 

       130        140        150        160        170        180 
VLLTLSPEAQ YQQSLDLTIT PEEEVQFIVT GSYAISLSGN YVKHPFDTPM GVEGEDEDED 

       190        200        210        220        230        240 
ADIYDSEDYD LTPDEDEIIG DDMDDLDDEE EEEVRIEEVQ EEDEEDNDGE EEQEEEEEEE 

       250        260        270        280        290        300 
QKEEVKPEPK KSKKEKKRKH EEKEEEKKAK KVKKVEFKKD LEEGPTKPKS KKEQDKHKPK 

       310        320        330        340        350        360 
SKVLEGGIVI EDRTIGDGPQ AKRGARVGMR YIGKLKNGKV FDKNTSGKPF AFKLGRGEVI 

       370        380        390        400        410 
KGWDIGVAGM SVGGERRIII PAPYAYGKQA LPGIPANSEL TFDVKLVSMK N 

« Hide

References

« Hide 'large scale' references
[1]"Purification of FKBP-70, a novel immunophilin from Saccharomyces cerevisiae, and cloning of its structural gene, FPR3."
Manning-Krieg U.C., Henriquez R., Cammas F., Graff P., Gaveriaux S., Movva N.R.
FEBS Lett. 352:98-103(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus."
Shan X., Xue Z., Melese T.
J. Cell Biol. 126:853-862(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus."
Benton B.M., Zang J.-H., Thorner J.
J. Cell Biol. 127:623-639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YNN 214.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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. 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.
[7]"Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3."
Wilson L.K., Dhillon N., Thorner J., Martin G.S.
J. Biol. Chem. 272:12961-12967(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-184 AND SER-186.
[8]"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].
[9]"Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein."
Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D.
Biochem. J. 388:819-826(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOP53, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"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-80 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-80; SER-81 AND THR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34569 Genomic DNA. Translation: AAB04165.1.
X79379 Genomic DNA. Translation: CAA55924.1.
S73876 Genomic DNA. Translation: AAB31995.1.
Z46373 Genomic DNA. Translation: CAA86504.1.
AY693136 Genomic DNA. Translation: AAT93155.1.
BK006946 Genomic DNA. Translation: DAA09823.1.
PIRS48647.
RefSeqNP_013637.1. NM_001182433.1.

3D structure databases

ProteinModelPortalP38911.
SMRP38911. Positions 266-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35067. 71 interactions.
DIPDIP-6578N.
IntActP38911. 59 interactions.
MINTMINT-673400.
STRING4932.YML074C.

Proteomic databases

MaxQBP38911.
PaxDbP38911.
PeptideAtlasP38911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML074C; YML074C; YML074C.
GeneID854901.
KEGGsce:YML074C.

Organism-specific databases

CYGDYML074c.
SGDS000004539. FPR3.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00530000064286.
HOGENOMHOG000216214.
KOK14826.
OMAKGECIKG.
OrthoDBEOG77WWQ3.

Enzyme and pathway databases

BioCycYEAST:YML074C-MONOMER.

Gene expression databases

GenevestigatorP38911.

Family and domain databases

InterProIPR026257. FK506_BP.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PIRSFPIRSF001473. FK506-bp_FPR3. 1 hit.
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977879.

Entry information

Entry nameFKBP3_YEAST
AccessionPrimary (citable) accession number: P38911
Secondary accession number(s): D6W0K9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 130 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 XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families