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P40454 (PTPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A activator 1

EC=5.2.1.8
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase PTPA-1
Short name=PPIase PTPA-1
Short name=Rotamase PTPA-1
Phosphotyrosyl phosphatase activator 1
Gene names
Name:RRD1
Synonyms:NCS1, YPA1
Ordered Locus Names:YIL153W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg2+ by dissociating the inactive form from the complex. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair. Ref.3 Ref.4 Ref.5 Ref.8 Ref.10 Ref.11

Catalytic activity

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

Subunit structure

Interacts with the phosphatase PP2A-like catalytic subunits PPG1, PPH3 and SIT4. Forms a ternary complex with SIT4-TAP42. Ref.4 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.6 Ref.8.

Miscellaneous

Present with 4590 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PTPA-type PPIase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PSY2P401643EBI-25278,EBI-29107
SIT4P206044EBI-25278,EBI-13707

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Serine/threonine-protein phosphatase 2A activator 1
PRO_0000202955

Amino acid modifications

Modified residue3411Phosphoserine Ref.12 Ref.13

Experimental info

Mutagenesis2051D → G: Abolishes PPIase activity and fails to activate PP2A phosphatases. Ref.11

Secondary structure

................................................. 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40454 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 22F52B3359739B6E

FASTA39345,082
        10         20         30         40         50         60 
MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS HCSDPDPHAT 

        70         80         90        100        110        120 
ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE WHHKLDERLP QWLQEMLPSE 

       130        140        150        160        170        180 
YHEVVPELQY YLGNSFGSST RLDYGTGHEL SFMATVAALD MLGMFPHMRG ADVFLLFNKY 

       190        200        210        220        230        240 
YTIMRRLILT YTLEPAGSHG VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR 

       250        260        270        280        290        300 
EYKDTNFYCQ GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP 

       310        320        330        340        350        360 
VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR FPTSTSMPPP 

       370        380        390 
GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations."
Van Hoof C., Janssens V., De Baere I., Stark M.J.R., de Winde J.H., Winderickx J., Thevelein J.M., Merlevede W., Goris J.
Exp. Cell Res. 264:372-387(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae."
Mitchell D.A., Sprague G.F. Jr.
Mol. Cell. Biol. 21:488-500(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIT4.
[5]"A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo."
Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I., Zaragoza K., Juno C., Ogris E.
Genes Dev. 17:2138-2150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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].
[8]"The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA."
Douville J., David J., Fortier P.K., Ramotar D.
Curr. Genet. 46:72-81(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIT4.
[9]"Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2."
Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V., Goris J.
Biochem. J. 386:93-102(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPG1; PPH3 AND SIT4.
[10]"The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes."
Zheng Y., Jiang Y.
Mol. Biol. Cell 16:2119-2127(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIT4 AND TAP42.
[11]"The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase."
Jordens J., Janssens V., Longin S., Stevens I., Martens E., Bultynck G., Engelborghs Y., Lescrinier E., Waelkens E., Goris J., Van Hoof C.
J. Biol. Chem. 281:6349-6357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-205.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38059 Genomic DNA. Translation: CAA86125.1.
BK006942 Genomic DNA. Translation: DAA08400.1.
PIRS48381.
RefSeqNP_012113.1. NM_001179501.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXOX-ray2.60A/B1-317[»]
2IXPX-ray2.80A/B/C/D1-317[»]
ProteinModelPortalP40454.
SMRP40454. Positions 2-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34839. 127 interactions.
DIPDIP-5663N.
IntActP40454. 20 interactions.
MINTMINT-520859.
STRING4932.YIL153W.

Proteomic databases

PaxDbP40454.
PeptideAtlasP40454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL153W; YIL153W; YIL153W.
GeneID854653.
KEGGsce:YIL153W.

Organism-specific databases

CYGDYIL153w.
SGDS000001415. RRD1.

Phylogenomic databases

eggNOGCOG5057.
GeneTreeENSGT00390000011500.
HOGENOMHOG000205736.
KOK17605.
OMAHELSFMA.
OrthoDBEOG76HQD0.

Enzyme and pathway databases

BioCycYEAST:G3O-31402-MONOMER.

Gene expression databases

GenevestigatorP40454.

Family and domain databases

InterProIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERPTHR10012. PTHR10012. 1 hit.
PfamPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFPIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40454.
NextBio977208.
PROP40454.

Entry information

Entry namePTPA1_YEAST
AccessionPrimary (citable) accession number: P40454
Secondary accession number(s): D6VVD4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references