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P23594

- PP2A1_YEAST

UniProt

P23594 - PP2A1_YEAST

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Protein

Serine/threonine-protein phosphatase PP2A-1 catalytic subunit

Gene

PPH21

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi117 – 1171Manganese 1By similarity
Metal bindingi119 – 1191Manganese 1By similarity
Metal bindingi145 – 1451Manganese 1By similarity
Metal bindingi145 – 1451Manganese 2By similarity
Metal bindingi177 – 1771Manganese 2By similarity
Active sitei178 – 1781Proton donorBy similarity
Metal bindingi227 – 2271Manganese 2By similarity
Metal bindingi301 – 3011Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. actin filament organization Source: SGD
  2. budding cell bud growth Source: SGD
  3. G1/S transition of mitotic cell cycle Source: SGD
  4. mitotic spindle assembly checkpoint Source: SGD
  5. protein dephosphorylation Source: SGD
  6. regulation of translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29532-MONOMER.
ReactomeiREACT_229625. Glycolysis.
REACT_230393. Integration of energy metabolism.
REACT_231087. ERK/MAPK targets.
REACT_241060. ERKs are inactivated.
REACT_261338. PP2A-mediated dephosphorylation of key metabolic factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A-1 catalytic subunit (EC:3.1.3.16)
Gene namesi
Name:PPH21
Ordered Locus Names:YDL134C
ORF Names:D2180
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL134c.
SGDiS000002292. PPH21.

Subcellular locationi

GO - Cellular componenti

  1. protein phosphatase type 2A complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991L → A: Reduced interaction with TAP42. 1 Publication
Mutagenesisi102 – 1021E → A: Reduced interaction with TAP42. 1 Publication
Mutagenesisi103 – 1031E → A: Reduced interaction with TAP42. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Serine/threonine-protein phosphatase PP2A-1 catalytic subunitPRO_0000058873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei369 – 3691Leucine methyl ester1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP23594.
PaxDbiP23594.
PeptideAtlasiP23594.

Expressioni

Gene expression databases

GenevestigatoriP23594.

Interactioni

Subunit structurei

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-TAP42.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAP42Q043726EBI-12745,EBI-18926

Protein-protein interaction databases

BioGridi31927. 133 interactions.
DIPiDIP-2282N.
IntActiP23594. 13 interactions.
MINTiMINT-534242.
STRINGi4932.YDL134C.

Structurei

3D structure databases

ProteinModelPortaliP23594.
SMRiP23594. Positions 69-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
InParanoidiP23594.
KOiK04382.
OMAiGVECAAS.
OrthoDBiEOG7FFN29.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23594-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDTDLDVPMQ DAVTEQLTPT VSEDMDLNNN SSDNNAEEFS VDDLKPGSSG
60 70 80 90 100
IADHKSSKPL ELNNTNINQL DQWIEHLSKC EPLSEDDVAR LCKMAVDVLQ
110 120 130 140 150
FEENVKPINV PVTICGDVHG QFHDLLELFK IGGPCPDTNY LFMGDYVDRG
160 170 180 190 200
YYSVETVSYL VAMKVRYPHR ITILRGNHES RQITQVYGFY DECLRKYGSA
210 220 230 240 250
NVWKMFTDLF DYFPITALVD NKIFCLHGGL SPMIETIDQV RELNRIQEVP
260 270 280 290 300
HEGPMCDLLW SDPDDRGGWG ISPRGAGFTF GQDVSEQFNH TNDLSLIARA
310 320 330 340 350
HQLVMEGYAW SHQQNVVTIF SAPNYCYRCG NQAAIMEVDE NHNRQFLQYD
360
PSVRPGEPSV SRKTPDYFL
Length:369
Mass (Da):41,938
Last modified:November 1, 1991 - v1
Checksum:iD8D5757283C9BBD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA41525. PABY21.
RefSeqiNP_010147.1. NM_001180193.1.

Genome annotation databases

EnsemblFungiiYDL134C; YDL134C; YDL134C.
GeneIDi851421.
KEGGisce:YDL134C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A41525. PABY21.
RefSeqi NP_010147.1. NM_001180193.1.

3D structure databases

ProteinModelPortali P23594.
SMRi P23594. Positions 69-352.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31927. 133 interactions.
DIPi DIP-2282N.
IntActi P23594. 13 interactions.
MINTi MINT-534242.
STRINGi 4932.YDL134C.

Proteomic databases

MaxQBi P23594.
PaxDbi P23594.
PeptideAtlasi P23594.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL134C ; YDL134C ; YDL134C .
GeneIDi 851421.
KEGGi sce:YDL134C.

Organism-specific databases

CYGDi YDL134c.
SGDi S000002292. PPH21.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074618.
HOGENOMi HOG000172696.
InParanoidi P23594.
KOi K04382.
OMAi GVECAAS.
OrthoDBi EOG7FFN29.

Enzyme and pathway databases

BioCyci YEAST:G3O-29532-MONOMER.
Reactomei REACT_229625. Glycolysis.
REACT_230393. Integration of energy metabolism.
REACT_231087. ERK/MAPK targets.
REACT_241060. ERKs are inactivated.
REACT_261338. PP2A-mediated dephosphorylation of key metabolic factors.

Miscellaneous databases

NextBioi 968624.

Gene expression databases

Genevestigatori P23594.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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 AT LEU-369 BY PPM1, DEMETHYLATION AT LEU-369 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. 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.

Entry informationi

Entry nameiPP2A1_YEAST
AccessioniPrimary (citable) accession number: P23594
Secondary accession number(s): D6VRL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 138 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 5620 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3