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

Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit

Gene

ppa2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis, possibly acting as an inhibitor.

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 bindingi70 – 701Manganese 1By similarity
Metal bindingi72 – 721Manganese 1By similarity
Metal bindingi98 – 981Manganese 1By similarity
Metal bindingi98 – 981Manganese 2By similarity
Metal bindingi130 – 1301Manganese 2By similarity
Active sitei131 – 1311Proton donorBy similarity
Metal bindingi180 – 1801Manganese 2By similarity
Metal bindingi254 – 2541Manganese 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: PomBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  • protein dephosphorylation Source: PomBase
  • signal transduction Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_292227. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_304275. Glycolysis.
REACT_309729. Integration of energy metabolism.
REACT_315486. ERK/MAPK targets.
REACT_328317. ERKs are inactivated.

Names & Taxonomyi

Protein namesi
Recommended name:
Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit (EC:3.1.3.16)
Gene namesi
Name:ppa2
ORF Names:SPBC16H5.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.07c.
PomBaseiSPBC16H5.07c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Major serine/threonine-protein phosphatase PP2A-2 catalytic subunitPRO_0000058872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei322 – 3221Leucine methyl esterBy similarity

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP23636.
PaxDbiP23636.

Interactioni

Protein-protein interaction databases

BioGridi276610. 100 interactions.
MINTiMINT-4687798.
STRINGi4896.SPBC16H5.07c-1.

Structurei

3D structure databases

ProteinModelPortaliP23636.
SMRiP23636. Positions 22-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiP23636.
KOiK04382.
OMAiRRITCAS.
OrthoDBiEOG7FFN29.
PhylomeDBiP23636.

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.

P23636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDPANDSK LAPEANDATL GDVDRWIEQL KKCEPLSEAD VEMLCDKARE
60 70 80 90 100
VLCQENNVQP VRNPVTVCGD IHGQFHDLME LFKIGGDVPD MNYLFMGDYV
110 120 130 140 150
DRGYHSVETV SLLVAMKLRY PNRITILRGN HESRQITQVY GFYDECLRKY
160 170 180 190 200
GSANVWKHFT NLFDYFPLTA LIEDRIFCLH GGLSPSIDSL DHVRTLDRVQ
210 220 230 240 250
EVPHEGPMCD LLWSDPDDRC GWGISPRGAG YTFGQDISET FNHANGLSLT
260 270 280 290 300
ARAHQLVMEG FNWAHDGDVV TIFSAPNYCY RCGNQAAILE VDDTMNQVFL
310 320
QFDPAPREGE PVIARRTPDY FL
Length:322
Mass (Da):36,489
Last modified:November 1, 1991 - v1
Checksum:i8709C544FAFEDD85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58519 Genomic DNA. Translation: AAA63579.1.
CU329671 Genomic DNA. Translation: CAA17905.1.
PIRiB36076.
RefSeqiNP_595940.1. NM_001021848.2.

Genome annotation databases

EnsemblFungiiSPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
GeneIDi2540072.
KEGGispo:SPBC16H5.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58519 Genomic DNA. Translation: AAA63579.1.
CU329671 Genomic DNA. Translation: CAA17905.1.
PIRiB36076.
RefSeqiNP_595940.1. NM_001021848.2.

3D structure databases

ProteinModelPortaliP23636.
SMRiP23636. Positions 22-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276610. 100 interactions.
MINTiMINT-4687798.
STRINGi4896.SPBC16H5.07c-1.

Proteomic databases

MaxQBiP23636.
PaxDbiP23636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
GeneIDi2540072.
KEGGispo:SPBC16H5.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.07c.
PomBaseiSPBC16H5.07c.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
InParanoidiP23636.
KOiK04382.
OMAiRRITCAS.
OrthoDBiEOG7FFN29.
PhylomeDBiP23636.

Enzyme and pathway databases

ReactomeiREACT_292227. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_304275. Glycolysis.
REACT_309729. Integration of energy metabolism.
REACT_315486. ERK/MAPK targets.
REACT_328317. ERKs are inactivated.

Miscellaneous databases

NextBioi20801209.
PROiP23636.

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. "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.

Entry informationi

Entry nameiPP2A2_SCHPO
AccessioniPrimary (citable) accession number: P23636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 27, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Retarded cell growth is produced by disruption of ppa2.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.