Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23635 (PP2A1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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:
Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit

EC=3.1.3.16
Gene names
Name:ppa1
ORF Names:SPAC823.15
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length309 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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
PRO_0000058871

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Amino acid modifications

Modified residue3091Leucine methyl ester By similarity

Sequences

Sequence LengthMass (Da)Tools
P23635 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 0F47604E5F740B0C

FASTA30935,291
        10         20         30         40         50         60 
MSVSGKIGEV DRWIEQLSRC EPLSEEDVIQ MCDLAKEVLS VESNVQSVRC PVTVCGDIHG 

        70         80         90        100        110        120 
QFHDLMELFN IGGPSPDTNY LFMGDYVDRG YHSVETVSLL IAFKIRYPQR ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWQYFTDLF DYLPLTALIE DRIFCLHGGL SPSIDTLDHV 

       190        200        210        220        230        240 
RILDRVQEVP HEGPICDLLW SDPDDRPGWG ISPRGAGYTF GPDIAEAFNH NNGLDLIARA 

       250        260        270        280        290        300 
HQLVMEGYNW TTNHNVVTIF SAPNYCYRCG NQAAIMGIDD HINYAFIQYD TAPRKEELHV 


TRRTPDYFL 

« 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]"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
M58518 Genomic DNA. Translation: AAA63578.1.
CU329670 Genomic DNA. Translation: CAB90160.1.
PIRA36076.
RefSeqNP_593842.1. NM_001019271.2.

3D structure databases

ProteinModelPortalP23635.
SMRP23635. Positions 9-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278531. 12 interactions.
MINTMINT-4687784.
STRING4896.SPAC823.15-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC823.15.1; SPAC823.15.1:pep; SPAC823.15.
GeneID2542052.
KEGGspo:SPAC823.15.

Organism-specific databases

PomBaseSPAC823.15.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
KOK04382.
OMAVENDIFC.
PhylomeDBP23635.

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

NextBio20803127.

Entry information

Entry namePP2A1_SCHPO
AccessionPrimary (citable) accession number: P23635
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 107 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