P23595 (PP2A2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exact function not known, phosphatase 2A performs an essential cellular function.
Catalytic activity	A phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from genetic interaction PubMed 12518319. Source: SGD actin filament organization Traceable author statement PubMed 9001215. Source: SGD budding cell bud growth Traceable author statement PubMed 9001215. Source: SGD mitotic spindle assembly checkpoint Inferred from physical interaction PubMed 9001215. Source: SGD protein dephosphorylation Inferred from direct assay PubMed 12135475. Source: SGD regulation of translation Inferred from physical interaction PubMed 10329624. Source: SGD
Cellular_component	condensed nuclear chromosome, centromeric region Inferred from direct assay PubMed 16541024. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 12135475. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAP42	Q04372	5	EBI-12752,EBI-18926
TIP41	Q12199	3	EBI-12752,EBI-38123

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Serine/threonine-protein phosphatase PP2A-2 catalytic subunit		PRO_0000058874
Sites
	Active site	186	1	Proton donor By similarity
	Metal binding	125	1	Iron By similarity
	Metal binding	127	1	Iron By similarity
	Metal binding	153	1	Iron By similarity
	Metal binding	153	1	Manganese By similarity
	Metal binding	185	1	Manganese By similarity
	Metal binding	235	1	Manganese By similarity
	Metal binding	309	1	Manganese By similarity
Amino acid modifications
	Modified residue	43	1	Phosphothreonine Ref.12 Ref.13 Ref.15
	Modified residue	56	1	Phosphoserine Ref.14 Ref.15
	Modified residue	377	1	Leucine methyl ester

Sequences

	Sequence		Length	Mass (Da)
	P23595 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 549D3C6F1E2EB335	FASTA	377	43,047
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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 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 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, MASS SPECTROMETRY. Strain: ADR376.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, MASS SPECTROMETRY.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY.
[15]	"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 AND SER-56, MASS SPECTROMETRY.
+	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.
PIR	PABY22. B41525.
RefSeq	NP_010093.1. NM_001180248.1.
3D structure databases
ProteinModelPortal	P23595.
SMR	P23595. Positions 43-360.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2283N.
IntAct	P23595. 38 interactions.
MINT	MINT-499723.
STRING	4932.YDL188C.
Proteomic databases
PaxDb	P23595.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL188C; YDL188C; YDL188C.
GeneID	851339.
KEGG	sce:YDL188C.
Organism-specific databases
CYGD	YDL188c.
SGD	S000002347. PPH22.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00550000074618.
HOGENOM	HOG000172696.
KO	K04382.
OrthoDB	EOG4GTPNM.
Gene expression databases
Genevestigator	P23595.
GermOnline	YDL188C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968414.

Entry information

Entry name

PP2A2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program