P23636 (PP2A2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
EC=3.1.3.16

Gene names

Name:	ppa2
ORF Names:	SPBC16H5.07c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis, possibly acting as an inhibitor.
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.
Miscellaneous	Retarded cell growth is produced by disruption of ppa2.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2A subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Methylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of G2/M transition of mitotic cell cycle Inferred from mutant phenotype PubMed 22624651. Source: PomBase protein dephosphorylation Inferred from mutant phenotype Ref.1. Source: PomBase signal transduction Non-traceable author statement. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from mutant phenotype Ref.1. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit		PRO_0000058872
Sites
	Active site	131	1	Proton donor By similarity
	Metal binding	70	1	Iron By similarity
	Metal binding	72	1	Iron By similarity
	Metal binding	98	1	Iron By similarity
	Metal binding	98	1	Manganese By similarity
	Metal binding	130	1	Manganese By similarity
	Metal binding	180	1	Manganese By similarity
	Metal binding	254	1	Manganese By similarity
Amino acid modifications
	Modified residue	322	1	Leucine methyl ester By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23636 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 8709C544FAFEDD85	FASTA	322	36,489
	10 20 30 40 50 60 MSIDPANDSK LAPEANDATL GDVDRWIEQL KKCEPLSEAD VEMLCDKARE VLCQENNVQP 70 80 90 100 110 120 VRNPVTVCGD IHGQFHDLME LFKIGGDVPD MNYLFMGDYV DRGYHSVETV SLLVAMKLRY 130 140 150 160 170 180 PNRITILRGN HESRQITQVY GFYDECLRKY GSANVWKHFT NLFDYFPLTA LIEDRIFCLH 190 200 210 220 230 240 GGLSPSIDSL DHVRTLDRVQ EVPHEGPMCD LLWSDPDDRC GWGISPRGAG YTFGQDISET 250 260 270 280 290 300 FNHANGLSLT ARAHQLVMEG FNWAHDGDVV TIFSAPNYCY RCGNQAAILE VDDTMNQVFL 310 320 QFDPAPREGE PVIARRTPDY FL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle." Kinoshita N., Ohkura H., Yanagida M. Cell 63:405-415(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / HM123.
[2]	"DNA sequencing and analysis of a 67.4 kb region from the right arm of Schizosaccharomyces pombe chromosome II reveals 28 open reading frames including the genes his5, pol5, ppa2, rip1, rpb8 and skb1." Xiang Z., Lyne M.H., Wood V., Rajandream M.A., Barrell B.G., Aves S.J. Yeast 15:893-901(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58519 Genomic DNA. Translation: AAA63579.1. CU329671 Genomic DNA. Translation: CAA17905.1.
PIR	B36076.
RefSeq	NP_595940.1. NM_001021848.2.
3D structure databases
ProteinModelPortal	P23636.
SMR	P23636. Positions 22-322.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC16H5.07c-1.
Proteomic databases
PaxDb	P23636.
PRIDE	P23636.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
GeneID	2540072.
KEGG	spo:SPBC16H5.07c.
Organism-specific databases
PomBase	SPBC16H5.07c.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172696.
KO	K04382.
OMA	TFNHANR.
OrthoDB	EOG4GTPNM.
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	20801209.

Entry information

Entry name

PP2A2_SCHPO

Accession

Primary (citable) accession number: P23636

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program