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Q9P7H1 (FLP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. 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:
Tyrosine-protein phosphatase CDC14 homolog

EC=3.1.3.48
Alternative name(s):
CDC fourteen-like phosphatase 1
Gene names
Name:clp1
Synonyms:flp1
ORF Names:SPAC1782.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase which antagonizes mitotic cyclin-dependent kinase cdc2, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Dephosphorylates the mitotic inducer cdc25 for its rapid degradation. Down-regulation of cdc25 activity ensures a prompt inactivation of mitotic cdc2 complexes to trigger cell division. Dephosphorylates also cdc2-phosphorylated nsk1, allowing nsk1-binding to kinetochores and spindle. Dephosphorylates ase1, which is essential for spindle midzone assembly and for continuous extension of the anaphase spindle. Tethered to the contractile ring by mid1, where it dephosphorylates cdc15. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with ark1 at the kinetochores. Interacts with bir1, cdc25, mid1, nbl1, pic1, and rad24. Ref.4 Ref.5 Ref.7 Ref.11 Ref.12

Subcellular location

Nucleusnucleolus. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body. Cell septum. Note: Localizes to kinetochores in prometaphase. Cytoplasmic retention is mediated through the binding of rad24. Tethered to the contractile ring by mid1. Ref.2 Ref.3 Ref.4 Ref.7 Ref.8 Ref.11 Ref.12 Ref.15

Post-translational modification

Phosphorylated by cds1, chk1, pmk1, and cdc2 upon Hydroxylurea and H2O2 stress treatment. Phosphorylation regulates the nucleolar-to-nucleoplasmic transition. Is able to autodephosphorylate. Ref.3 Ref.15

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Meiosis
Mitosis
Septation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactomyosin contractile ring maintenance

Inferred from mutant phenotype Ref.11. Source: PomBase

attachment of spindle microtubules to kinetochore

Inferred from genetic interaction Ref.4. Source: PomBase

barrier septum assembly

Inferred from mutant phenotype Ref.3. Source: PomBase

cellular protein localization

Inferred from mutant phenotype Ref.4. Source: PomBase

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.15. Source: PomBase

cellular response to hydrogen peroxide

Inferred from mutant phenotype Ref.15. Source: PomBase

chromosome passenger complex localization to spindle midzone

Inferred from mutant phenotype Ref.12. Source: PomBase

cytokinesis checkpoint

Inferred from mutant phenotype Ref.2Ref.6. Source: PomBase

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cytokinesis

Non-traceable author statement. Source: PomBase

mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.4. Source: PomBase

negative regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.14. Source: PomBase

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from genetic interaction Ref.3. Source: PomBase

positive regulation of attachment of spindle microtubules to kinetochore involved in mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.13. Source: PomBase

positive regulation of septation initiation signaling

Traceable author statement Ref.3. Source: PomBase

protein dephosphorylation

Inferred by curator. Source: PomBase

regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.2. Source: PomBase

regulation of exit from mitosis

Inferred from mutant phenotype Ref.5. Source: PomBase

sister chromatid biorientation

Inferred from mutant phenotype Ref.4. Source: PomBase

   Cellular_componentcell septum

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed nuclear chromosome kinetochore

Inferred from direct assay Ref.4. Source: PomBase

cytoplasm

Inferred from direct assay Ref.2. Source: PomBase

medial cortex

Inferred from direct assay Ref.2. Source: PomBase

mitotic spindle pole body

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

nucleolus

Inferred from direct assay Ref.2Ref.15. Source: PomBase

nucleoplasm

Inferred from direct assay Ref.15. Source: PomBase

nucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

   Molecular_functionphosphoprotein phosphatase activity

Inferred from direct assay Ref.5PubMed 19686686PubMed 23297348. Source: PomBase

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.13PubMed 23297348. Source: PomBase

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rad24P426563EBI-704737,EBI-704791

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 537537Tyrosine-protein phosphatase CDC14 homolog
PRO_0000094874

Sites

Active site2861Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue4531Phosphothreonine Ref.9
Modified residue4681Phosphoserine Ref.9
Modified residue4701Phosphoserine Ref.9
Modified residue5131Phosphoserine Ref.9

Experimental info

Mutagenesis2861C → A: Inactivates phosphatase activity. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Q9P7H1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F5E50A8C0924C7EA

FASTA53760,253
        10         20         30         40         50         60 
MDYQDDGLGE MIEFLEDKLY YTSLSQPPKA ELYPHMHFFT IDDELIYNPF YHDFGPLNVS 

        70         80         90        100        110        120 
HLIRFAVIVH GIMGKHRQAK KSKAIVLYSS TDTRLRANAA CLLACYMVLV QNWPPHLALA 

       130        140        150        160        170        180 
PLAQAEPPFL GFRDAGYAVS DYYITIQDCV YGLWRARESS ILNIRNIDVH DYETYERVEN 

       190        200        210        220        230        240 
GDFNWISPKF IAFASPIQAG WNHASTRPKK LPQPFAIVLD YFVANKVKLI VRLNGPLYDK 

       250        260        270        280        290        300 
KTFENVGIRH KEMYFEDGTV PELSLVKEFI DLTEEVEEDG VIAVHCKAGL GRTGCLIGAY 

       310        320        330        340        350        360 
LIYKHCFTAN EVIAYMRIMR PGMVVGPQQH WLHINQVHFR AYFYEKAMGR AIQQATAAEP 

       370        380        390        400        410        420 
LATPPRHPLN ATNGTSQSNI STPLPEPTPG QPRKVSGHNP PSARRLPSAS SVKFNEKLKN 

       430        440        450        460        470        480 
ASKQSIQNEN KASYSSYEDS EIQNDDETRT VGTPTETISV VRLRRSSSQS NIEPNGVRSP 

       490        500        510        520        530 
TSSPTGSPIR RTSGNRWSSG SSHSKKSAQR SVSMSSLNNT SNGRVAKPKP SKSRLIS 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Fission yeast Clp1p phosphatase regulates G2/M transition and coordination of cytokinesis with cell cycle progression."
Trautmann S., Wolfe B.A., Jorgensen P., Tyers M., Gould K.L., McCollum D.
Curr. Biol. 11:931-940(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[3]"Flp1, a fission yeast orthologue of the s. cerevisiae CDC14 gene, is not required for cyclin degradation or rum1p stabilisation at the end of mitosis."
Cueille N., Salimova E., Esteban V., Blanco M., Moreno S., Bueno A., Simanis V.
J. Cell Sci. 114:2649-2664(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[4]"The S. pombe Cdc14-like phosphatase Clp1p regulates chromosome biorientation and interacts with Aurora kinase."
Trautmann S., Rajagopalan S., McCollum D.
Dev. Cell 7:755-762(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARK1.
[5]"A role for the Cdc14-family phosphatase Flp1p at the end of the cell cycle in controlling the rapid degradation of the mitotic inducer Cdc25p in fission yeast."
Esteban V., Blanco M., Cueille N., Simanis V., Moreno S., Bueno A.
J. Cell Sci. 117:2461-2468(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF CDC25, INTERACTION WITH CDC25.
[6]"The Clp1p/Flp1p phosphatase ensures completion of cytokinesis in response to minor perturbation of the cell division machinery in Schizosaccharomyces pombe."
Mishra M., Karagiannis J., Trautmann S., Wang H., McCollum D., Balasubramanian M.K.
J. Cell Sci. 117:3897-3910(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The 14-3-3 protein rad24p modulates function of the cdc14p family phosphatase clp1p/flp1p in fission yeast."
Mishra M., Karagiannis J., Sevugan M., Singh P., Balasubramanian M.K.
Curr. Biol. 15:1376-1383(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD24, SUBCELLULAR LOCATION.
[8]"Distinct nuclear and cytoplasmic functions of the S. pombe Cdc14-like phosphatase Clp1p/Flp1p and a role for nuclear shuttling in its regulation."
Trautmann S., McCollum D.
Curr. Biol. 15:1384-1389(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453; SER-468; SER-470 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Cdc14-regulated midzone assembly controls anaphase B."
Khmelinskii A., Lawrence C., Roostalu J., Schiebel E.
J. Cell Biol. 177:981-993(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF ASE1, MUTAGENESIS OF CYS-286.
[11]"The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by association with anillin-related Mid1."
Clifford D.M., Wolfe B.A., Roberts-Galbraith R.H., McDonald W.H., Yates J.R. III, Gould K.L.
J. Cell Biol. 181:79-88(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MID1, SUBCELLULAR LOCATION, FUNCTION IN DEPHOSPHORYLATION OF CDC15.
[12]"A link between aurora kinase and Clp1/Cdc14 regulation uncovered by the identification of a fission yeast borealin-like protein."
Bohnert K.A., Chen J.S., Clifford D.M., Vander Kooi C.W., Gould K.L.
Mol. Biol. Cell 20:3646-3659(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIR1; NBL1 AND PIC1, FUNCTION, SUBCELLULAR LOCATION.
[13]"Cdk1 phosphorylation of the kinetochore protein Nsk1 prevents error-prone chromosome segregation."
Chen J.S., Lu L.X., Ohi M.D., Creamer K.M., English C., Partridge J.F., Ohi R., Gould K.L.
J. Cell Biol. 195:583-593(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF NSK1.
[14]"A systematic screen reveals new elements acting at the G2/M cell cycle control."
Navarro F.J., Nurse P.
Genome Biol. 13:R36.1-R36.10(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Multiple protein kinases influence the redistribution of fission yeast Clp1/Cdc14 phosphatase upon genotoxic stress."
Broadus M.R., Gould K.L.
Mol. Biol. Cell 23:4118-4128(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB76271.1.
PIRT50099.
RefSeqNP_594716.1. NM_001020143.2.

3D structure databases

ProteinModelPortalQ9P7H1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278823. 237 interactions.
IntActQ9P7H1. 4 interactions.
MINTMINT-4705468.
STRING4896.SPAC1782.09c-1.

Proteomic databases

MaxQBQ9P7H1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1782.09c.1; SPAC1782.09c.1:pep; SPAC1782.09c.
GeneID2542358.
KEGGspo:SPAC1782.09c.

Organism-specific databases

PomBaseSPAC1782.09c.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000198341.
KOK06639.
OMANDDETRT.
PhylomeDBQ9P7H1.

Family and domain databases

Gene3D3.90.190.10. 2 hits.
InterProIPR026070. CDC14.
IPR029260. DSPn.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803418.
PROQ9P7H1.

Entry information

Entry nameFLP1_SCHPO
AccessionPrimary (citable) accession number: Q9P7H1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 116 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