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P13681 (PP11_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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 PP1-1

EC=3.1.3.16
Gene names
Name:dis2
Synonyms:bws1
ORF Names:SPBC776.02c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis.

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.

Subunit structure

Oligomer.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from genetic interaction PubMed 14765108. Source: PomBase

microtubule cytoskeleton organization

Inferred from genetic interaction PubMed 3428262. Source: PomBase

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein dephosphorylation

Inferred from direct assay PubMed 14765108. Source: PomBase

rRNA processing

Inferred from sequence orthology. Source: PomBase

regulation of homologous chromosome segregation

Inferred from mutant phenotype Ref.2. Source: PomBase

regulation of mitotic cell cycle

Inferred from genetic interaction Ref.5. Source: PomBase

signal transduction

Non-traceable author statement. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16823372. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

mRNA cleavage and polyadenylation specificity factor complex

Inferred from direct assay PubMed 14617822. Source: PomBase

nucleus

Inferred from direct assay PubMed 16823372Ref.2. Source: PomBase

protein phosphatase type 1 complex

Inferred from sequence orthology Ref.2. Source: PomBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 14765108. Source: PomBase

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.4. Source: PomBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tea4O601322EBI-4320127,EBI-1099982

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Serine/threonine-protein phosphatase PP1-1
PRO_0000058818

Sites

Active site1241Proton donor By similarity
Metal binding631Iron By similarity
Metal binding651Iron By similarity
Metal binding911Iron By similarity
Metal binding911Manganese By similarity
Metal binding1231Manganese By similarity
Metal binding1721Manganese By similarity
Metal binding2471Manganese By similarity

Amino acid modifications

Modified residue3161Phosphothreonine; by CDC2

Experimental info

Mutagenesis2451R → Q: Cold-sensitive phenotype.
Sequence conflict171E → EGE Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13681 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 1106BB9C7D6FDCFB

FASTA32737,636
        10         20         30         40         50         60 
MSNPDVDLDS IIDRLLEVRG SRPGRQVQLS EDEIRFLCNK AREIFISQPI LLELEAPLKI 

        70         80         90        100        110        120 
CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL EVICLLLAYK IKYPENFFIL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN 

       190        200        210        220        230        240 
SMDQIQRIMR PTDVPDTGLL CDLLWSDPDK DLTGWGDNDR GVSFTFGPDV VSRFLHKHDM 

       250        260        270        280        290        300 
DLVCRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK 

       310        320 
KQRYGYQGSS QNWHMTPPRK NKTGNSK 

« Hide

References

« Hide 'large scale' references
[1]"Involvement of a type 1 protein phosphatase encoded by bws1+ in fission yeast mitotic control."
Booher R., Beach D.
Cell 57:1009-1016(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SP557.
[2]"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases."
Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.
Cell 57:997-1007(1989) [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]"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: MUTANT CS.
Strain: 972 / HM123.
[5]"Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regulation."
Yamano H., Ishii K., Yanagida M.
EMBO J. 13:5310-5318(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27075 Genomic DNA. Translation: AAA74731.1.
M27068 Genomic DNA. Translation: AAA89197.1.
CU329671 Genomic DNA. Translation: CAA22875.1.
PIRA32550.
RefSeqNP_596317.1. NM_001022239.2.

3D structure databases

ProteinModelPortalP13681.
SMRP13681. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277707. 63 interactions.
IntActP13681. 2 interactions.
MINTMINT-4687271.
STRING4896.SPBC776.02c-1.

Proteomic databases

PaxDbP13681.
PRIDEP13681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC776.02c.1; SPBC776.02c.1:pep; SPBC776.02c.
GeneID2541193.
KEGGspo:SPBC776.02c.

Organism-specific databases

PomBaseSPBC776.02c.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
KOK06269.
OMALEHEIRY.
OrthoDBEOG79KPQ9.
PhylomeDBP13681.

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

NextBio20802305.

Entry information

Entry namePP11_SCHPO
AccessionPrimary (citable) accession number: P13681
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 124 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