Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein phosphatase PP2A-2 catalytic subunit

Gene

PPH22

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

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 bindingi125 – 1251Manganese 1By similarity
Metal bindingi127 – 1271Manganese 1By similarity
Metal bindingi153 – 1531Manganese 1By similarity
Metal bindingi153 – 1531Manganese 2By similarity
Metal bindingi185 – 1851Manganese 2By similarity
Active sitei186 – 1861Proton donorBy similarity
Metal bindingi235 – 2351Manganese 2By similarity
Metal bindingi309 – 3091Manganese 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. negative regulation of ribonucleoprotein complex localization Source: SGD
  6. peptidyl-serine dephosphorylation Source: SGD
  7. protein dephosphorylation Source: SGD
  8. 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-29573-MONOMER.
ReactomeiREACT_275254. Glycolysis.
REACT_302117. ERK/MAPK targets.
REACT_311526. ERKs are inactivated.
REACT_317166. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_347913. Integration of energy metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A-2 catalytic subunit (EC:3.1.3.16)
Gene namesi
Name:PPH22
Synonyms:SIS4
Ordered Locus Names:YDL188C
ORF Names:D1271
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL188c.
SGDiS000002347. PPH22.

Subcellular locationi

GO - Cellular componenti

  1. condensed nuclear chromosome, centromeric region Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Serine/threonine-protein phosphatase PP2A-2 catalytic subunitPRO_0000058874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei43 – 431Phosphothreonine3 Publications
Modified residuei377 – 3771Leucine methyl ester2 Publications

Post-translational modificationi

Reversibly methyl esterified on Leu-377 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, Phosphoprotein

Proteomic databases

MaxQBiP23595.
PaxDbiP23595.

Expressioni

Gene expression databases

GenevestigatoriP23595.

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. Interacts with TAP42.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HMT1P380743EBI-12752,EBI-8394
TAP42Q043724EBI-12752,EBI-18926
TIP41Q121993EBI-12752,EBI-38123

Protein-protein interaction databases

BioGridi31857. 103 interactions.
DIPiDIP-2283N.
IntActiP23595. 28 interactions.
MINTiMINT-499723.
STRINGi4932.YDL188C.

Structurei

3D structure databases

ProteinModelPortaliP23595.
SMRiP23595. Positions 43-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
InParanoidiP23595.
KOiK04382.
OMAiMHGSDED.
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.

P23595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMEIDDPMH GSDEDQLSPT LDEDMNSDDG KNNTKARSND EDTDEELEDF
60 70 80 90 100
NFKPGSSGIA DHKSSKPLKL TNTNINQLDQ WIEHLSKCEP LSEDDVARLC
110 120 130 140 150
KMAVDVLQFE ENVKPINVPV TICGDVHGQF HDLLELFKIG GPCPDTNYLF
160 170 180 190 200
MGDYVDRGYY SVETVSYLVA MKVRYPHRIT ILRGNHESRQ ITQVYGFYDE
210 220 230 240 250
CLRKYGSANV WKMFTDLFDY FPVTALVDNK IFCLHGGLSP MIETIDQVRD
260 270 280 290 300
LNRIQEVPHE GPMCDLLWSD PDDRGGWGIS PRGAGFTFGQ DISEQFNHTN
310 320 330 340 350
DLSLIARAHQ LVMEGYSWSH QQNVVTIFSA PNYCYRCGNQ AAIMEVDENH
360 370
NRQFLQYDPS VRPGEPTVTR KTPDYFL
Length:377
Mass (Da):43,047
Last modified:November 1, 1991 - v1
Checksum:i549D3C6F1E2EB335
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56262 Genomic DNA. Translation: CAA39703.1.
M60317 Genomic DNA. Translation: AAB04032.1.
X58857 Genomic DNA. Translation: CAA41659.1.
X83276 Genomic DNA. Translation: CAA58259.1.
Z74236 Genomic DNA. Translation: CAA98765.1.
BK006938 Genomic DNA. Translation: DAA11675.1.
PIRiB41525. PABY22.
RefSeqiNP_010093.1. NM_001180248.1.

Genome annotation databases

EnsemblFungiiYDL188C; YDL188C; YDL188C.
GeneIDi851339.
KEGGisce:YDL188C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56262 Genomic DNA. Translation: CAA39703.1.
M60317 Genomic DNA. Translation: AAB04032.1.
X58857 Genomic DNA. Translation: CAA41659.1.
X83276 Genomic DNA. Translation: CAA58259.1.
Z74236 Genomic DNA. Translation: CAA98765.1.
BK006938 Genomic DNA. Translation: DAA11675.1.
PIRiB41525. PABY22.
RefSeqiNP_010093.1. NM_001180248.1.

3D structure databases

ProteinModelPortaliP23595.
SMRiP23595. Positions 43-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31857. 103 interactions.
DIPiDIP-2283N.
IntActiP23595. 28 interactions.
MINTiMINT-499723.
STRINGi4932.YDL188C.

Proteomic databases

MaxQBiP23595.
PaxDbiP23595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL188C; YDL188C; YDL188C.
GeneIDi851339.
KEGGisce:YDL188C.

Organism-specific databases

CYGDiYDL188c.
SGDiS000002347. PPH22.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
InParanoidiP23595.
KOiK04382.
OMAiMHGSDED.
OrthoDBiEOG7FFN29.

Enzyme and pathway databases

BioCyciYEAST:G3O-29573-MONOMER.
ReactomeiREACT_275254. Glycolysis.
REACT_302117. ERK/MAPK targets.
REACT_311526. ERKs are inactivated.
REACT_317166. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_347913. Integration of energy metabolism.

Miscellaneous databases

NextBioi968414.

Gene expression databases

GenevestigatoriP23595.

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]
ProtoNetiSearch...

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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LL20.
  2. "The SIT4 protein phosphatase functions in late G1 for progression into S phase."
    Sutton A., Immanuel D., Arndt K.T.
    Mol. Cell. Biol. 11:2133-2148(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 208353 / W303-1A.
  4. "New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
    Verhasselt P., Voet M., Volckaert G.
    Yeast 11:961-966(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  5. "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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LEU-377 BY PPM1, DEMETHYLATION BY PPE1.
  8. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LEU-377 BY PPM1.
  9. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAP42.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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 PPE1 AND RRD2.
  12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "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 THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-38 AND THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP2A2_YEAST
AccessioniPrimary (citable) accession number: P23595
Secondary accession number(s): D6VRG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 1, 2015
This is version 147 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 4110 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

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.