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P23595 (PP2A2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. 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-2 catalytic subunit

EC=3.1.3.16
Gene names
Name:PPH22
Synonyms:SIS4
Ordered Locus Names:YDL188C
ORF Names:D1271
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length377 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. Interacts with TAP42. Ref.9 Ref.11

Post-translational modification

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.

Miscellaneous

Present with 4110 molecules/cell in log phase SD medium.

Sequence similarities

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
PRO_0000058874

Sites

Active site1861Proton donor By similarity
Metal binding1251Iron By similarity
Metal binding1271Iron By similarity
Metal binding1531Iron By similarity
Metal binding1531Manganese By similarity
Metal binding1851Manganese By similarity
Metal binding2351Manganese By similarity
Metal binding3091Manganese By similarity

Amino acid modifications

Modified residue381Phosphoserine Ref.14
Modified residue431Phosphothreonine Ref.12 Ref.13 Ref.14
Modified residue3771Leucine methyl ester Ref.7 Ref.8

Sequences

Sequence LengthMass (Da)Tools
P23595 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 549D3C6F1E2EB335

FASTA37743,047
        10         20         30         40         50         60 
MDMEIDDPMH GSDEDQLSPT LDEDMNSDDG KNNTKARSND EDTDEELEDF NFKPGSSGIA 

        70         80         90        100        110        120 
DHKSSKPLKL TNTNINQLDQ WIEHLSKCEP LSEDDVARLC KMAVDVLQFE ENVKPINVPV 

       130        140        150        160        170        180 
TICGDVHGQF HDLLELFKIG GPCPDTNYLF MGDYVDRGYY SVETVSYLVA MKVRYPHRIT 

       190        200        210        220        230        240 
ILRGNHESRQ ITQVYGFYDE CLRKYGSANV WKMFTDLFDY FPVTALVDNK IFCLHGGLSP 

       250        260        270        280        290        300 
MIETIDQVRD LNRIQEVPHE GPMCDLLWSD PDDRGGWGIS PRGAGFTFGQ DISEQFNHTN 

       310        320        330        340        350        360 
DLSLIARAHQ LVMEGYSWSH QQNVVTIFSA PNYCYRCGNQ AAIMEVDENH NRQFLQYDPS 

       370 
VRPGEPTVTR KTPDYFL 

« 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]"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(1991) [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(1991) [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(1995) [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. 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.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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(2000) [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(2001) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAP42.
[10]"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].
[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(2005) [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(2007) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPABY22. B41525.
RefSeqNP_010093.1. NM_001180248.1.

3D structure databases

ProteinModelPortalP23595.
SMRP23595. Positions 43-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31857. 97 interactions.
DIPDIP-2283N.
IntActP23595. 28 interactions.
MINTMINT-499723.
STRING4932.YDL188C.

Proteomic databases

PaxDbP23595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL188C; YDL188C; YDL188C.
GeneID851339.
KEGGsce:YDL188C.

Organism-specific databases

CYGDYDL188c.
SGDS000002347. PPH22.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
HOGENOMHOG000172696.
KOK04382.
OMASANVWKI.
OrthoDBEOG7FFN29.

Enzyme and pathway databases

BioCycYEAST:G3O-29573-MONOMER.

Gene expression databases

GenevestigatorP23595.

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

NextBio968414.

Entry information

Entry namePP2A2_YEAST
AccessionPrimary (citable) accession number: P23595
Secondary accession number(s): D6VRG5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 139 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