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Q12461 (PTPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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:
Serine/threonine-protein phosphatase 2A activator 2

EC=5.2.1.8
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase PTPA-2
Short name=PPIase PTPA-2
Short name=Rotamase PTPA-2
Phosphotyrosyl phosphatase activator 2
Gene names
Name:RRD2
Synonyms:NOH1, YPA2
Ordered Locus Names:YPL152W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length358 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. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis. Ref.4 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11

Catalytic activity

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

Subunit structure

Interacts with the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms a ternary complex with PPH21-TAP42. Ref.6 Ref.9 Ref.10

Subcellular location

Cytoplasm Ref.7.

Miscellaneous

Present with 2430 molecules/cell in log phase SD medium.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Serine/threonine-protein phosphatase 2A activator 2
PRO_0000226120

Secondary structure

............................................. 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12461 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E0BE8A7EDD54E306

FASTA35841,452
        10         20         30         40         50         60 
MLPEKRLLTP DDMKLWEESP TRAHFTKFII DLAESVKGHE NSQYKEPISE SINSMMNLLS 

        70         80         90        100        110        120 
QIKDITQKHP VIKDADSSRF GKVEFRDFYD EVSRNSRKIL RSEFPSLTDE QLEQLSIYLD 

       130        140        150        160        170        180 
ESWGNKRRID YGSGHELNFM CLLYGLYSYG IFNLSNDSTN LVLKVFIEYL KIMRILETKY 

       190        200        210        220        230        240 
WLEPAGSHGV WGLDDYHFLP FLFGAFQLTT HKHLKPISIH NNELVEMFAH RYLYFGCIAF 

       250        260        270        280        290        300 
INKVKSSASL RWHSPMLDDI SGVKTWSKVA EGMIKMYKAE VLSKLPIMQH FYFSEFLPCP 

       310        320        330        340        350 
DGVSPPRGHI HDGTDKDDEC NFEGHVHTTW GDCCGIKLPS AIAATEMNKK HHKPIPFD 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators."
Purnelle B., Coster F., Goffeau A.
Yeast 12:1483-1492(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"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.
[6]"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, INTERACTION WITH PPH21.
[7]"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].
[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]"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: FUNCTION, INTERACTION WITH PPH21 AND PPH22.
[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 PPH21 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96770 Genomic DNA. Translation: CAA65569.1.
Z73508 Genomic DNA. Translation: CAA97857.1.
BK006949 Genomic DNA. Translation: DAA11283.1.
PIRS65163.
RefSeqNP_015173.1. NM_001183966.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXNX-ray2.80A/B1-304[»]
ProteinModelPortalQ12461.
SMRQ12461. Positions 3-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36031. 62 interactions.
DIPDIP-2558N.
IntActQ12461. 3 interactions.
MINTMINT-556521.
STRING4932.YPL152W.

Proteomic databases

PaxDbQ12461.
PeptideAtlasQ12461.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL152W; YPL152W; YPL152W.
GeneID855951.
KEGGsce:YPL152W.

Organism-specific databases

CYGDYPL152w.
SGDS000006073. RRD2.

Phylogenomic databases

eggNOGCOG5057.
HOGENOMHOG000205736.
KOK17605.
OMAFRTFYDK.
OrthoDBEOG76HQD0.

Enzyme and pathway databases

BioCycYEAST:G3O-34049-MONOMER.

Gene expression databases

GenevestigatorQ12461.

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

EvolutionaryTraceQ12461.
NextBio980732.
PROQ12461.

Entry information

Entry namePTPA2_YEAST
AccessionPrimary (citable) accession number: Q12461
Secondary accession number(s): D6W3L7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 101 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 XVI

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

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references