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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

Miscellaneous

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

Catalytic activityi

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

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: SGD
  • protein phosphatase regulator activity Source: SGD
  • protein tyrosine phosphatase activator activity Source: GO_Central

GO - Biological processi

  • DNA repair Source: SGD
  • G1/S transition of mitotic cell cycle Source: SGD
  • mitotic spindle organization in nucleus Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  • response to osmotic stress Source: SGD

Keywordsi

Molecular functionIsomerase, 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
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL153W.
SGDiS000001415. RRD1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi205D → G: Abolishes PPIase activity and fails to activate PP2A phosphatases. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002029551 – 393Serine/threonine-protein phosphatase 2A activator 1Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei341PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40454.
PRIDEiP40454.

PTM databases

iPTMnetiP40454.

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

Show more details

Protein-protein interaction databases

BioGridi34839. 246 interactors.
DIPiDIP-5663N.
IntActiP40454. 50 interactors.
MINTiMINT-520859.
STRINGi4932.YIL153W.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 10Combined sources3
Helixi23 – 28Combined sources6
Helixi29 – 31Combined sources3
Helixi33 – 49Combined sources17
Helixi65 – 79Combined sources15
Helixi97 – 116Combined sources20
Helixi119 – 124Combined sources6
Helixi125 – 133Combined sources9
Turni139 – 141Combined sources3
Helixi146 – 161Combined sources16
Helixi170 – 190Combined sources21
Helixi200 – 202Combined sources3
Beta strandi205 – 207Combined sources3
Helixi210 – 218Combined sources9
Beta strandi220 – 222Combined sources3
Helixi223 – 225Combined sources3
Beta strandi226 – 228Combined sources3
Helixi230 – 234Combined sources5
Helixi236 – 242Combined sources7
Turni243 – 245Combined sources3
Helixi247 – 258Combined sources12
Helixi263 – 266Combined sources4
Helixi268 – 274Combined sources7
Helixi280 – 294Combined sources15
Turni295 – 297Combined sources3
Helixi299 – 302Combined sources4
Beta strandi309 – 312Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP40454.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPA-type PPIase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000011500.
HOGENOMiHOG000205736.
InParanoidiP40454.
KOiK17605.
OMAiNEHSPII.
OrthoDBiEOG092C3CMG.

Family and domain databases

CDDicd04087. PTPA. 1 hit.
InterProiView protein in InterPro
IPR004327. Phstyr_phstse_ac.
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiView protein in Pfam
PF03095. PTPA. 1 hit.
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.

Similar proteinsi

Entry informationi

Entry nameiPTPA1_YEAST
AccessioniPrimary (citable) accession number: P40454
Secondary accession number(s): D6VVD4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 27, 2017
This is version 152 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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