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P36614 (PPE1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase ppe1

EC=3.1.3.16
Alternative name(s):
Phosphatase esp1
Gene names
Name:ppe1
Synonyms:esp1, ppx1
ORF Names:SPCC1739.12
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. Negatively regulates mis12. Ref.4

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Interacts with sts5, ekc1 and mis12. Ref.4

Subcellular location

Nucleus. Note: Associated with chromatin. Ref.4

Sequence similarities

Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Cell shape
Mitosis
   Cellular componentNucleus
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from sequence or structural similarity Ref.1. Source: GOC

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of hydroxymethylglutaryl-CoA reductase (NADPH) activity

Inferred from mutant phenotype PubMed 21680738. Source: PomBase

positive regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway

Inferred from mutant phenotype PubMed 21680738. Source: PomBase

positive regulation of protein dephosphorylation

Inferred from mutant phenotype PubMed 21680738. Source: PomBase

regulation of cell shape

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.4. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nuclear chromatin

Inferred from direct assay Ref.4. Source: PomBase

nucleus

Inferred from direct assay Ref.4PubMed 16823372. Source: PomBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from sequence or structural similarity Ref.1. Source: PomBase

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ekc1O745112EBI-1153118,EBI-1153096

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Serine/threonine-protein phosphatase ppe1
PRO_0000058882

Sites

Active site1121Proton donor By similarity
Metal binding511Manganese 1 By similarity
Metal binding531Manganese 1 By similarity
Metal binding791Manganese 1 By similarity
Metal binding791Manganese 2 By similarity
Metal binding1111Manganese 2 By similarity
Metal binding1611Manganese 2 By similarity
Metal binding2351Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P36614 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 001980A1CC7646D7

FASTA30535,259
        10         20         30         40         50         60 
MFDLDEWIAT VRKCKYLPEH QLKRLCEMVK VILMEESNIQ PVRTPVTVCG DIHGQFYDLL 

        70         80         90        100        110        120 
ELFRVGGELP STNYIFMGDF VDRGYFSLET FTLFMLLKAR YPDKITLLRG NHESRQITQV 

       130        140        150        160        170        180 
YGFYDECQTK YGNANVWKYC CQVFDFLTLA AVIDNKILCV HGGLSPEVRT LDQIRILARA 

       190        200        210        220        230        240 
QEIPHEGSFC DLMWSDPEDI ESWTVSPRGA GWLFGSKVTT EFSQINDLTL IARAHQLVQE 

       250        260        270        280        290        300 
GYKYHFADKN LVTVWSAPNY CYRCGNVASV MKVDESLEPE FRIFSAVADE DRTVPPSRKR 


SEYFI 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the fission yeast protein phosphatase gene ppe1+ involved in cell shape control and mitosis."
Shimanuki M., Kinoshita N., Ohkura H., Yoshida T., Toda T., Yanagida M.
Mol. Biol. Cell 4:303-313(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / HM123.
[2]"Interaction of the pim1/spi1 mitotic checkpoint with a protein phosphatase."
Matsumoto T., Beach D.
Mol. Biol. Cell 4:337-345(1993) [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.
[4]"The role of Ppe1/PP6 phosphatase for equal chromosome segregation in fission yeast kinetochore."
Goshima G., Iwasaki O., Obuse C., Yanagida M.
EMBO J. 22:2752-2763(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STS5; ECK1 AND MIS12, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13712 Genomic DNA. Translation: BAA02865.1.
Z18925 Genomic DNA. Translation: CAA79358.1.
CU329672 Genomic DNA. Translation: CAA20786.1.
PIRA47727.
RefSeqNP_588420.1. NM_001023411.2.

3D structure databases

ProteinModelPortalP36614.
SMRP36614. Positions 3-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275341. 32 interactions.
IntActP36614. 2 interactions.
MINTMINT-4689011.
STRING4896.SPCC1739.12-1.

Proteomic databases

MaxQBP36614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1739.12.1; SPCC1739.12.1:pep; SPCC1739.12.
GeneID2538758.
KEGGspo:SPCC1739.12.

Organism-specific databases

PomBaseSPCC1739.12.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
KOK15427.
OMAGELLCVH.
OrthoDBEOG7FFN29.
PhylomeDBP36614.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20799942.
PROP36614.

Entry information

Entry namePPE1_SCHPO
AccessionPrimary (citable) accession number: P36614
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 122 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