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Protein

Serine/threonine-protein phosphatase 2A activator 1

Gene

RRD1

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. 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.6 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: SGD
  2. phosphatase activator activity Source: InterPro
  3. protein phosphatase type 2A regulator activity Source: SGD

GO - Biological processi

  1. DNA repair Source: SGD
  2. G1/S transition of mitotic cell cycle Source: SGD
  3. mitotic spindle organization in nucleus Source: SGD
  4. protein peptidyl-prolyl isomerization Source: GOC
  5. regulation of catalytic activity Source: GOC
  6. regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  7. response to osmotic stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:G3O-31402-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RRD1
Synonyms:NCS1, YPA1
Ordered Locus Names:YIL153W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IX

Organism-specific databases

CYGDiYIL153w.
SGDiS000001415. RRD1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051D → G: Abolishes PPIase activity and fails to activate PP2A phosphatases. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Serine/threonine-protein phosphatase 2A activator 1PRO_0000202955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei341 – 3411Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40454.
PaxDbiP40454.
PeptideAtlasiP40454.

Expressioni

Gene expression databases

GenevestigatoriP40454.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PSY2P401643EBI-25278,EBI-29107
SIT4P206044EBI-25278,EBI-13707

Protein-protein interaction databases

BioGridi34839. 129 interactions.
DIPiDIP-5663N.
IntActiP40454. 20 interactions.
MINTiMINT-520859.
STRINGi4932.YIL153W.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Helixi23 – 286Combined sources
Helixi29 – 313Combined sources
Helixi33 – 4917Combined sources
Helixi65 – 7915Combined sources
Helixi97 – 11620Combined sources
Helixi119 – 1246Combined sources
Helixi125 – 1339Combined sources
Turni139 – 1413Combined sources
Helixi146 – 16116Combined sources
Helixi170 – 19021Combined sources
Helixi200 – 2023Combined sources
Beta strandi205 – 2073Combined sources
Helixi210 – 2189Combined sources
Beta strandi220 – 2223Combined sources
Helixi223 – 2253Combined sources
Beta strandi226 – 2283Combined sources
Helixi230 – 2345Combined sources
Helixi236 – 2427Combined sources
Turni243 – 2453Combined sources
Helixi247 – 25812Combined sources
Helixi263 – 2664Combined sources
Helixi268 – 2747Combined sources
Helixi280 – 29415Combined sources
Turni295 – 2973Combined sources
Helixi299 – 3024Combined sources
Beta strandi309 – 3124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXOX-ray2.60A/B1-317[»]
2IXPX-ray2.80A/B/C/D1-317[»]
ProteinModelPortaliP40454.
SMRiP40454. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40454.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPA-type PPIase family.Curated

Phylogenomic databases

eggNOGiCOG5057.
GeneTreeiENSGT00780000122340.
HOGENOMiHOG000205736.
InParanoidiP40454.
KOiK17605.
OMAiHELSFMA.
OrthoDBiEOG76HQD0.

Family and domain databases

InterProiIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

P40454-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS
60 70 80 90 100
HCSDPDPHAT ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE
110 120 130 140 150
WHHKLDERLP QWLQEMLPSE YHEVVPELQY YLGNSFGSST RLDYGTGHEL
160 170 180 190 200
SFMATVAALD MLGMFPHMRG ADVFLLFNKY YTIMRRLILT YTLEPAGSHG
210 220 230 240 250
VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR EYKDTNFYCQ
260 270 280 290 300
GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP
310 320 330 340 350
VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR
360 370 380 390
FPTSTSMPPP GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR
Length:393
Mass (Da):45,082
Last modified:February 1, 1995 - v1
Checksum:i22F52B3359739B6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86125.1.
BK006942 Genomic DNA. Translation: DAA08400.1.
PIRiS48381.
RefSeqiNP_012113.1. NM_001179501.1.

Genome annotation databases

EnsemblFungiiYIL153W; YIL153W; YIL153W.
GeneIDi854653.
KEGGisce:YIL153W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86125.1.
BK006942 Genomic DNA. Translation: DAA08400.1.
PIRiS48381.
RefSeqiNP_012113.1. NM_001179501.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXOX-ray2.60A/B1-317[»]
2IXPX-ray2.80A/B/C/D1-317[»]
ProteinModelPortaliP40454.
SMRiP40454. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34839. 129 interactions.
DIPiDIP-5663N.
IntActiP40454. 20 interactions.
MINTiMINT-520859.
STRINGi4932.YIL153W.

Proteomic databases

MaxQBiP40454.
PaxDbiP40454.
PeptideAtlasiP40454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL153W; YIL153W; YIL153W.
GeneIDi854653.
KEGGisce:YIL153W.

Organism-specific databases

CYGDiYIL153w.
SGDiS000001415. RRD1.

Phylogenomic databases

eggNOGiCOG5057.
GeneTreeiENSGT00780000122340.
HOGENOMiHOG000205736.
InParanoidiP40454.
KOiK17605.
OMAiHELSFMA.
OrthoDBiEOG76HQD0.

Enzyme and pathway databases

BioCyciYEAST:G3O-31402-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40454.
NextBioi977208.
PROiP40454.

Gene expression databases

GenevestigatoriP40454.

Family and domain databases

InterProiIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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(2000) [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(2000) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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(2003) [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(2004) [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(2004) [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(2005) [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(2007) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTPA1_YEAST
AccessioniPrimary (citable) accession number: P40454
Secondary accession number(s): D6VVD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4590 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

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 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.