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Q9P7H1 (FLP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 105. 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

Has a role in regulating entry into mitosis and promotes septum signaling. Ref.2

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Nucleusnucleolus. Cytoplasmcytoskeletonspindle pole body. Note: Until mitosis and the spindle pole body through to late anaphase. Ref.2

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
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 PubMed 18378776. Source: PomBase

barrier septum assembly involved in cell cycle cytokinesis

Inferred from mutant phenotype Ref.2. Source: PomBase

chromosome passenger complex localization to spindle midzone

Inferred from mutant phenotype PubMed 19570910. Source: PomBase

cytokinesis checkpoint

Inferred from mutant phenotype PubMed 11448769PubMed 15265986. Source: PomBase

negative regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 22624651. Source: PomBase

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

Inferred from genetic interaction Ref.2. Source: PomBase

peptidyl-tyrosine dephosphorylation

Inferred from electronic annotation. Source: GOC

positive regulation of septation initiation signaling cascade

Traceable author statement Ref.2. Source: PomBase

regulation of exit from mitosis

Inferred from mutant phenotype PubMed 15128870. Source: PomBase

sister chromatid biorientation

Inferred from mutant phenotype PubMed 15525536. Source: PomBase

   Cellular_componentcondensed nuclear chromosome kinetochore

Inferred from direct assay PubMed 15525536. Source: PomBase

medial cortex

Inferred from direct assay PubMed 11448769. Source: PomBase

mitotic spindle pole body

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleolus

Inferred from direct assay PubMed 11448769. Source: PomBase

   Molecular_functionphosphoprotein phosphatase activity

Inferred from direct assay PubMed 15128870PubMed 19666868. Source: PomBase

protein phosphatase inhibitor activity

Inferred from direct assay PubMed 15128870. Source: PomBase

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: 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.3
Modified residue4681Phosphoserine Ref.3
Modified residue4701Phosphoserine Ref.3
Modified residue5131Phosphoserine Ref.3

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]"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.
[3]"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, MASS SPECTROMETRY.
+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...

Protein-protein interaction databases

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

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.
OrthoDBEOG4MD17S.

Family and domain databases

InterProIPR026070. CDC14.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF22. PTHR23339:SF22. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803418.

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: May 29, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families