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Q12705 (PP2B_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. 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:
Serine/threonine-protein phosphatase 2B catalytic subunit

EC=3.1.3.16
Gene names
Name:ppb1
ORF Names:SPBC1346.01c, SPBP4H10.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Appears to be involved in cytokinesis, mating, transport, nuclear and spindle pole body positioning, and cell shape.

Catalytic activity

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

Cofactor

Binds 1 Fe3+ ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCell shape
   LigandCalmodulin-binding
Iron
Manganese
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling

Inferred from mutant phenotype PubMed 16928959. Source: PomBase

cellular chloride ion homeostasis

Inferred from mutant phenotype PubMed 9427748. Source: PomBase

cellular response to salt stress

Inferred from mutant phenotype PubMed 21811607PubMed 9427748. Source: PomBase

cytosolic calcium ion homeostasis

Inferred from mutant phenotype PubMed 21811607. Source: PomBase

fungal-type cell wall organization or biogenesis

Inferred from genetic interaction PubMed 1095095. Source: PomBase

negative regulation of calcium ion transport into cytosol

Inferred from mutant phenotype PubMed 21811607. Source: PomBase

protein dephosphorylation

Inferred by curator. Source: PomBase

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of conjugation with cellular fusion

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of cytokinesis

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of establishment or maintenance of cell polarity regulating cell shape

Inferred from mutant phenotype Ref.1. Source: PomBase

spindle pole body localization

Inferred from mutant phenotype PubMed 1668885. Source: PomBase

   Cellular_componentcalcineurin complex

Inferred from sequence orthology. Source: PomBase

cell division site

Inferred from direct assay PubMed 16823372PubMed 23956092. Source: PomBase

cytoplasm

Inferred from direct assay PubMed 23956092. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

   Molecular_functioncalcium-dependent protein serine/threonine phosphatase activity

Inferred from mutant phenotype PubMed 16928959. Source: PomBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from direct assay PubMed 15657058. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554Serine/threonine-protein phosphatase 2B catalytic subunit
PRO_0000058835

Sites

Active site1801Proton donor By similarity
Metal binding1191Iron By similarity
Metal binding1211Iron By similarity
Metal binding1471Iron By similarity
Metal binding1471Zinc By similarity
Metal binding1791Zinc By similarity
Metal binding2281Zinc By similarity
Metal binding3101Zinc By similarity

Experimental info

Sequence conflict121I → T in BAA06081. Ref.1
Sequence conflict129 – 1302KL → EI in BAA06081. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12705 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: D27ACA21AE2F3E19

FASTA55463,714
        10         20         30         40         50         60 
MTSGPHNLED PIVRAIRQKN QAPSHDFTIF VQEDGSSVST LDRVVKNVQA PATYIPTDVE 

        70         80         90        100        110        120 
FFDINEPDKP DLHFLRNHFI REGRLSEEQT LYIIKKATEI LKSEDNLIEV DAPVTVCGDI 

       130        140        150        160        170        180 
HGQYYDLMKL FEVGGNPANT QYLFLGDYVD RGYFSIECLL YLWALKIWYP KTLWLLRGNH 

       190        200        210        220        230        240 
ECAHLTDYFT FKLECTHKYN IKVYEACLQS FNALPLAAIM NKQFLCVHGG LSPELHTLND 

       250        260        270        280        290        300 
IRMINRFCEP PTHGLMCDLL WSDPLEDFGS EKSNKHFIHN NVRGCSYFYS YQAVCTFLEN 

       310        320        330        340        350        360 
NNLLSVIRAH EAQDVGYRMY RKTKTTGFPS LMTIFSAPNY LDVYNNKAAV LKYENNVMNI 

       370        380        390        400        410        420 
RQFNCSPHPY WLPNFMDVFT WSLPFVGEKV SEMLISMLNI CSKEELYETD LKESAPTQHK 

       430        440        450        460        470        480 
QPAPSENENK ADQEIDIEAR RQIIKNKIMA IGRISRVFSV LREERESVSE LKNVSGTQRL 

       490        500        510        520        530        540 
PAGTLMLGAE GIKNAINSFD DARKLDIQNE RLPPSNSRRR STDLKAFEEV MNSSEDDTSI 

       550 
DHLVERFADK KSSL 

« Hide

References

« Hide 'large scale' references
[1]"A calcineurin-like gene ppb1+ in fission yeast: mutant defects in cytokinesis, cell polarity, mating and spindle pole body positioning."
Yoshida T., Toda T., Yanagida M.
J. Cell Sci. 107:1725-1735(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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
D28955 Genomic DNA. Translation: BAA06081.1.
CU329671 Genomic DNA. Translation: CAB83162.1.
PIRT45137.
T50310.
RefSeqNP_596178.1. NM_001022097.2.

3D structure databases

ProteinModelPortalQ12705.
SMRQ12705. Positions 38-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276568. 39 interactions.
MINTMINT-4700029.
STRING4896.SPBP4H10.04-1.

Proteomic databases

MaxQBQ12705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBP4H10.04.1; SPBP4H10.04.1:pep; SPBP4H10.04.
GeneID2540024.
KEGGspo:SPBP4H10.04.

Organism-specific databases

PomBaseSPBP4H10.04.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172699.
KOK04348.
OMARDECECK.
OrthoDBEOG77M8X9.
PhylomeDBQ12705.

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

NextBio20801167.

Entry information

Entry namePP2B_SCHPO
AccessionPrimary (citable) accession number: Q12705
Secondary accession number(s): Q9P7E4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: June 11, 2014
This is version 118 of the entry and version 2 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