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P23594 (PP2A1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP2A-1 catalytic subunit

EC=3.1.3.16
Gene names
Name:PPH21
Ordered Locus Names:YDL134C
ORF Names:D2180
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exact function not known, phosphatase 2A performs an essential cellular function.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD2, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Forms a ternary complex with RRD2-TAP42. Ref.8 Ref.10 Ref.11

Post-translational modification

Reversibly methyl esterified on Leu-369 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.

Miscellaneous

Present with 5620 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-2A subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAP42Q043726EBI-12745,EBI-18926

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
PRO_0000058873

Sites

Active site1781Proton donor By similarity
Metal binding1171Iron By similarity
Metal binding1191Iron By similarity
Metal binding1451Iron By similarity
Metal binding1451Manganese By similarity
Metal binding1771Manganese By similarity
Metal binding2271Manganese By similarity
Metal binding3011Manganese By similarity

Amino acid modifications

Modified residue3691Leucine methyl ester

Experimental info

Mutagenesis991L → A: Reduced interaction with TAP42. Ref.8
Mutagenesis1021E → A: Reduced interaction with TAP42. Ref.8
Mutagenesis1031E → A: Reduced interaction with TAP42. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P23594 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: D8D5757283C9BBD6

FASTA36941,938
        10         20         30         40         50         60 
MDTDLDVPMQ DAVTEQLTPT VSEDMDLNNN SSDNNAEEFS VDDLKPGSSG IADHKSSKPL 

        70         80         90        100        110        120 
ELNNTNINQL DQWIEHLSKC EPLSEDDVAR LCKMAVDVLQ FEENVKPINV PVTICGDVHG 

       130        140        150        160        170        180 
QFHDLLELFK IGGPCPDTNY LFMGDYVDRG YYSVETVSYL VAMKVRYPHR ITILRGNHES 

       190        200        210        220        230        240 
RQITQVYGFY DECLRKYGSA NVWKMFTDLF DYFPITALVD NKIFCLHGGL SPMIETIDQV 

       250        260        270        280        290        300 
RELNRIQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGFTF GQDVSEQFNH TNDLSLIARA 

       310        320        330        340        350        360 
HQLVMEGYAW SHQQNVVTIF SAPNYCYRCG NQAAIMEVDE NHNRQFLQYD PSVRPGEPSV 


SRKTPDYFL 

« Hide

References

« Hide 'large scale' references
[1]"Saccharomyces cerevisiae protein phosphatase 2A performs an essential cellular function and is encoded by two genes."
Sneddon A.A., Cohen P.T.W., Stark M.J.R.
EMBO J. 9:4339-4346(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LL20.
[2]"Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 208353 / W303-1A.
[3]"Analysis of a 26,756 bp segment from the left arm of yeast chromosome IV."
Woelfl S., Haneman V., Saluz H.P.
Yeast 12:1549-1554(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo."
Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.
EMBO J. 19:5672-5681(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION BY PPM1, DEMETHYLATION BY PPE1.
[7]"Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast."
Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.
Arch. Biochem. Biophys. 395:239-245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION BY PPM1.
[8]"Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases."
Wang H., Wang X., Jiang Y.
Mol. Biol. Cell 14:4342-4351(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAP42, MUTAGENESIS OF LEU-99; GLU-102 AND GLU-103.
[9]"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].
[10]"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 PPE1 AND RRD2.
[11]"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: INTERACTION WITH RRD2 AND TAP42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56261 Genomic DNA. Translation: CAA39702.1.
X58856 Genomic DNA. Translation: CAA41656.1.
X96876 Genomic DNA. Translation: CAA65625.1.
Z74182 Genomic DNA. Translation: CAA98707.1.
BK006938 Genomic DNA. Translation: DAA11724.1.
PIRPABY21. A41525.
RefSeqNP_010147.1. NM_001180193.1.

3D structure databases

ProteinModelPortalP23594.
SMRP23594. Positions 32-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31927. 130 interactions.
DIPDIP-2282N.
IntActP23594. 13 interactions.
MINTMINT-534242.
STRING4932.YDL134C.

Proteomic databases

PaxDbP23594.
PeptideAtlasP23594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL134C; YDL134C; YDL134C.
GeneID851421.
KEGGsce:YDL134C.

Organism-specific databases

CYGDYDL134c.
SGDS000002292. PPH21.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
HOGENOMHOG000172696.
KOK04382.
OMAFTRCSED.
OrthoDBEOG7FFN29.

Enzyme and pathway databases

BioCycYEAST:G3O-29532-MONOMER.

Gene expression databases

GenevestigatorP23594.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968624.

Entry information

Entry namePP2A1_YEAST
AccessionPrimary (citable) accession number: P23594
Secondary accession number(s): D6VRL4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 132 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 IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families