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P23636 (PP2A2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit

EC=3.1.3.16
Gene names
Name:ppa2
ORF Names:SPBC16H5.07c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred 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 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.

Miscellaneous

Retarded cell growth is produced by disruption of ppa2.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
PRO_0000058872

Sites

Active site1311Proton donor By similarity
Metal binding701Iron By similarity
Metal binding721Iron By similarity
Metal binding981Iron By similarity
Metal binding981Manganese By similarity
Metal binding1301Manganese By similarity
Metal binding1801Manganese By similarity
Metal binding2541Manganese By similarity

Amino acid modifications

Modified residue3221Leucine methyl ester By similarity

Sequences

Sequence LengthMass (Da)Tools
P23636 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 8709C544FAFEDD85

FASTA32236,489
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58519 Genomic DNA. Translation: AAA63579.1.
CU329671 Genomic DNA. Translation: CAA17905.1.
PIRB36076.
RefSeqNP_595940.1. NM_001021848.2.

3D structure databases

ProteinModelPortalP23636.
SMRP23636. Positions 22-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276610. 103 interactions.
MINTMINT-4687798.
STRING4896.SPBC16H5.07c-1.

Proteomic databases

PaxDbP23636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
GeneID2540072.
KEGGspo:SPBC16H5.07c.

Organism-specific databases

PomBaseSPBC16H5.07c.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
KOK04382.
OMALMACKQL.
OrthoDBEOG7FFN29.
PhylomeDBP23636.

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

NextBio20801209.

Entry information

Entry namePP2A2_SCHPO
AccessionPrimary (citable) accession number: P23636
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names