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Reviewed, UniProtKB/Swiss-Prot Q9P7H1 (FLP1_SCHPO)

Last modified January 19, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [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
Gene Ontology (GO)
   Biological processG2/M transition of mitotic cell cycle

Inferred from mutant phenotype. Source: GeneDB_SPombe

attachment of spindle microtubules to kinetochore

Inferred from genetic interaction. Source: GeneDB_SPombe

barrier septum formation Ref.2

Inferred from mutant phenotype. Source: GeneDB_SPombe

cellular protein localization

Inferred from genetic interaction. Source: GeneDB_SPombe

contractile ring maintenance involved in cytokinesis during cell cycle

Inferred from mutant phenotype. Source: GeneDB_SPombe

cytokinesis checkpoint

Inferred from mutant phenotype. Source: GeneDB_SPombe

negative regulation of cyclin-dependent protein kinase activity Ref.2

Inferred from genetic interaction. Source: GeneDB_SPombe

positive regulation of septation initiation signaling Ref.2

Traceable author statement. Source: GeneDB_SPombe

protein amino acid dephosphorylation

Inferred by curator. Source: GeneDB_SPombe

regulation of exit from mitosis

Inferred from mutant phenotype. Source: GeneDB_SPombe

sister chromatid biorientation

Inferred from mutant phenotype. Source: GeneDB_SPombe

   Cellular componentcondensed chromosome kinetochore

Inferred from direct assay. Source: GeneDB_SPombe

nucleolus

Inferred from direct assay. Source: GeneDB_SPombe

spindle pole body

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionphosphoprotein phosphatase inhibitor activity

Inferred from genetic interaction. Source: GeneDB_SPombe

protein binding

Inferred from physical interaction. Source: IntAct

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

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
Q9P7H1-1 [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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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: 11683392] [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: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453; SER-468; SER-470 AND SER-513, MASS SPECTROMETRY.

Cross-references

Sequence databases

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

3D structure databases

SMRQ9P7H1. Positions 2-339.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9P7H1. 4 interactions.
STRINGQ9P7H1.

Genome annotation databases

GeneID2542358.
GenomeReviewsGene locus clp1 in contig CU329670_GR.
KEGGspo:SPAC1782.09c.
NMPDRfig|4896.1.peg.4686.

Organism-specific databases

GeneDB_SpombeSPAC1782.09c.

Phylogenomic databases

eggNOGfuNOG04637.
HOGENOMHBG398632.
OMALACYMVL.
OrthoDBEOG96Q899.
PhylomeDBQ9P7H1.

Enzyme and pathway databases

BRENDA3.1.3.48. 653.

Gene expression databases

ArrayExpressQ9P7H1.

Family and domain databases

InterProIPR000387. Dual-sp/Tyr_phosphatase.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 19, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents