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Tyrosine-protein phosphatase CDC14 homolog (EC 3.1.3.48) (CDC fourteen-like phosphatase 1)

 FLP1_SCHPO              Reviewed;         537 AA.
Q9P7H1;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Tyrosine-protein phosphatase CDC14 homolog;
EC=3.1.3.48;
AltName: Full=CDC fourteen-like phosphatase 1;
Name=clp1; Synonyms=flp1; ORFNames=SPAC1782.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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., 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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11448769; DOI=10.1016/S0960-9822(01)00268-8;
Trautmann S., Wolfe B.A., Jorgensen P., Tyers M., Gould K.L.,
McCollum D.;
"Fission yeast Clp1p phosphatase regulates G2/M transition and
coordination of cytokinesis with cell cycle progression.";
Curr. Biol. 11:931-940(2001).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=11683392;
Cueille N., Salimova E., Esteban V., Blanco M., Moreno S., Bueno A.,
Simanis V.;
"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.";
J. Cell Sci. 114:2649-2664(2001).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARK1.
PubMed=15525536; DOI=10.1016/j.devcel.2004.10.006;
Trautmann S., Rajagopalan S., McCollum D.;
"The S. pombe Cdc14-like phosphatase Clp1p regulates chromosome
biorientation and interacts with Aurora kinase.";
Dev. Cell 7:755-762(2004).
[5]
FUNCTION IN DEPHOSPHORYLATION OF CDC25, AND INTERACTION WITH CDC25.
PubMed=15128870; DOI=10.1242/jcs.01107;
Esteban V., Blanco M., Cueille N., Simanis V., Moreno S., Bueno A.;
"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.";
J. Cell Sci. 117:2461-2468(2004).
[6]
FUNCTION.
PubMed=15265986; DOI=10.1242/jcs.01244;
Mishra M., Karagiannis J., Trautmann S., Wang H., McCollum D.,
Balasubramanian M.K.;
"The Clp1p/Flp1p phosphatase ensures completion of cytokinesis in
response to minor perturbation of the cell division machinery in
Schizosaccharomyces pombe.";
J. Cell Sci. 117:3897-3910(2004).
[7]
INTERACTION WITH RAD24, AND SUBCELLULAR LOCATION.
PubMed=16085489; DOI=10.1016/j.cub.2005.06.070;
Mishra M., Karagiannis J., Sevugan M., Singh P., Balasubramanian M.K.;
"The 14-3-3 protein rad24p modulates function of the cdc14p family
phosphatase clp1p/flp1p in fission yeast.";
Curr. Biol. 15:1376-1383(2005).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16085490; DOI=10.1016/j.cub.2005.06.039;
Trautmann S., McCollum D.;
"Distinct nuclear and cytoplasmic functions of the S. pombe Cdc14-like
phosphatase Clp1p/Flp1p and a role for nuclear shuttling in its
regulation.";
Curr. Biol. 15:1384-1389(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453; SER-468; SER-470
AND SER-513, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
[10]
FUNCTION IN DEPHOSPHORYLATION OF ASE1, AND MUTAGENESIS OF CYS-286.
PubMed=17562791; DOI=10.1083/jcb.200702145;
Khmelinskii A., Lawrence C., Roostalu J., Schiebel E.;
"Cdc14-regulated midzone assembly controls anaphase B.";
J. Cell Biol. 177:981-993(2007).
[11]
INTERACTION WITH MID1, SUBCELLULAR LOCATION, AND FUNCTION IN
DEPHOSPHORYLATION OF CDC15.
PubMed=18378776; DOI=10.1083/jcb.200709060;
Clifford D.M., Wolfe B.A., Roberts-Galbraith R.H., McDonald W.H.,
Yates J.R. III, Gould K.L.;
"The Clp1/Cdc14 phosphatase contributes to the robustness of
cytokinesis by association with anillin-related Mid1.";
J. Cell Biol. 181:79-88(2008).
[12]
INTERACTION WITH BIR1; NBL1 AND PIC1, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=19570910; DOI=10.1091/mbc.E09-04-0289;
Bohnert K.A., Chen J.S., Clifford D.M., Vander Kooi C.W., Gould K.L.;
"A link between aurora kinase and Clp1/Cdc14 regulation uncovered by
the identification of a fission yeast borealin-like protein.";
Mol. Biol. Cell 20:3646-3659(2009).
[13]
FUNCTION IN DEPHOSPHORYLATION OF NSK1.
PubMed=22065639; DOI=10.1083/jcb.201105074;
Chen J.S., Lu L.X., Ohi M.D., Creamer K.M., English C.,
Partridge J.F., Ohi R., Gould K.L.;
"Cdk1 phosphorylation of the kinetochore protein Nsk1 prevents error-
prone chromosome segregation.";
J. Cell Biol. 195:583-593(2011).
[14]
FUNCTION.
PubMed=22624651; DOI=10.1186/gb-2012-13-5-r36;
Navarro F.J., Nurse P.;
"A systematic screen reveals new elements acting at the G2/M cell
cycle control.";
Genome Biol. 13:R36.1-R36.10(2012).
[15]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=22918952; DOI=10.1091/mbc.E12-06-0475;
Broadus M.R., Gould K.L.;
"Multiple protein kinases influence the redistribution of fission
yeast Clp1/Cdc14 phosphatase upon genotoxic stress.";
Mol. Biol. Cell 23:4118-4128(2012).
-!- 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. {ECO:0000269|PubMed:11448769,
ECO:0000269|PubMed:11683392, ECO:0000269|PubMed:15128870,
ECO:0000269|PubMed:15265986, ECO:0000269|PubMed:15525536,
ECO:0000269|PubMed:16085490, ECO:0000269|PubMed:17562791,
ECO:0000269|PubMed:18378776, ECO:0000269|PubMed:19570910,
ECO:0000269|PubMed:22065639, ECO:0000269|PubMed:22624651}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Interacts with ark1 at the kinetochores. Interacts with
bir1, cdc25, mid1, nbl1, pic1, and rad24.
{ECO:0000269|PubMed:15128870, ECO:0000269|PubMed:15525536,
ECO:0000269|PubMed:16085489, ECO:0000269|PubMed:18378776,
ECO:0000269|PubMed:19570910}.
-!- INTERACTION:
P42656:rad24; NbExp=3; IntAct=EBI-704737, EBI-704791;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, cytoskeleton,
microtubule organizing center, spindle 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.
-!- PTM: Phosphorylated by cds1, chk1, pmk1, and cdc2 upon
Hydroxylurea and H(2)O(2) stress treatment. Phosphorylation
regulates the nucleolar-to-nucleoplasmic transition. Is able to
autodephosphorylate. {ECO:0000269|PubMed:11683392,
ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:22918952}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class CDC14 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CU329670; CAB76271.1; -; Genomic_DNA.
PIR; T50099; T50099.
RefSeq; NP_594716.1; NM_001020143.2.
ProteinModelPortal; Q9P7H1; -.
SMR; Q9P7H1; -.
BioGrid; 278823; 240.
IntAct; Q9P7H1; 4.
MINT; MINT-4705468; -.
STRING; 4896.SPAC1782.09c.1; -.
iPTMnet; Q9P7H1; -.
MaxQB; Q9P7H1; -.
PRIDE; Q9P7H1; -.
EnsemblFungi; SPAC1782.09c.1; SPAC1782.09c.1:pep; SPAC1782.09c.
GeneID; 2542358; -.
KEGG; spo:SPAC1782.09c; -.
EuPathDB; FungiDB:SPAC1782.09c; -.
PomBase; SPAC1782.09c; clp1.
HOGENOM; HOG000198341; -.
InParanoid; Q9P7H1; -.
KO; K06639; -.
OrthoDB; EOG092C2FOY; -.
PhylomeDB; Q9P7H1; -.
Reactome; R-SPO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
PRO; PR:Q9P7H1; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005826; C:actomyosin contractile ring; IDA:PomBase.
GO; GO:0032153; C:cell division site; IDA:PomBase.
GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:PomBase.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0000776; C:kinetochore; IDA:PomBase.
GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
GO; GO:0005730; C:nucleolus; IDA:PomBase.
GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0000922; C:spindle pole; IBA:GO_Central.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:PomBase.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:PomBase.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
GO; GO:0035853; P:chromosome passenger complex localization to spindle midzone; IMP:PomBase.
GO; GO:0098783; P:correction of merotelic kinetochore attachment, mitotic; IGI:PomBase.
GO; GO:1990975; P:establishment of protein localization to mitotic spindle pole body; IMP:PomBase.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
GO; GO:0071850; P:mitotic cell cycle arrest; IBA:GO_Central.
GO; GO:0044878; P:mitotic cytokinesis checkpoint; IMP:PomBase.
GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:PomBase.
GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IMP:PomBase.
GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:PomBase.
GO; GO:0031031; P:positive regulation of septation initiation signaling; IGI:PomBase.
GO; GO:0034501; P:protein localization to kinetochore; IMP:PomBase.
GO; GO:1904789; P:regulation of mitotic actomyosin contractile ring maintenance; IGI:PomBase.
GO; GO:1990598; P:repair of mitotic mono-orientation defects; IMP:PomBase.
GO; GO:0072479; P:response to mitotic cell cycle spindle assembly checkpoint signaling; IMP:PomBase.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR026070; CDC14.
InterPro; IPR029260; DSPn.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
Pfam; PF00782; DSPc; 1.
Pfam; PF14671; DSPn; 1.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Hydrolase; Meiosis; Mitosis; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome; Septation.
CHAIN 1 537 Tyrosine-protein phosphatase CDC14
homolog.
/FTId=PRO_0000094874.
ACT_SITE 286 286 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 453 453 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MUTAGEN 286 286 C->A: Inactivates phosphatase activity.
{ECO:0000269|PubMed:17562791}.
SEQUENCE 537 AA; 60253 MW; F5E50A8C0924C7EA CRC64;
MDYQDDGLGE MIEFLEDKLY YTSLSQPPKA ELYPHMHFFT IDDELIYNPF YHDFGPLNVS
HLIRFAVIVH GIMGKHRQAK KSKAIVLYSS TDTRLRANAA CLLACYMVLV QNWPPHLALA
PLAQAEPPFL GFRDAGYAVS DYYITIQDCV YGLWRARESS ILNIRNIDVH DYETYERVEN
GDFNWISPKF IAFASPIQAG WNHASTRPKK LPQPFAIVLD YFVANKVKLI VRLNGPLYDK
KTFENVGIRH KEMYFEDGTV PELSLVKEFI DLTEEVEEDG VIAVHCKAGL GRTGCLIGAY
LIYKHCFTAN EVIAYMRIMR PGMVVGPQQH WLHINQVHFR AYFYEKAMGR AIQQATAAEP
LATPPRHPLN ATNGTSQSNI STPLPEPTPG QPRKVSGHNP PSARRLPSAS SVKFNEKLKN
ASKQSIQNEN KASYSSYEDS EIQNDDETRT VGTPTETISV VRLRRSSSQS NIEPNGVRSP
TSSPTGSPIR RTSGNRWSSG SSHSKKSAQR SVSMSSLNNT SNGRVAKPKP SKSRLIS


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