Q9P7H1 (FLP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. Cytoplasm › cytoskeleton › spindle 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 process	Cell cycle Cell division Mitosis Septation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	attachment of spindle microtubules to kinetochore Inferred from genetic interaction. Source: GeneDB_Spombe barrier septum assembly involved in cell cycle cytokinesis Inferred from mutant phenotype. Source: GeneDB_Spombe chromosome passenger complex localization to spindle midzone Inferred from mutant phenotype. Source: GeneDB_Spombe contractile ring maintenance involved in cell cycle cytokinesis Inferred from mutant phenotype. Source: GeneDB_Spombe cytokinesis checkpoint Inferred from mutant phenotype. Source: GeneDB_Spombe negative regulation of cyclin-dependent protein kinase activity Inferred from genetic interaction. Source: GeneDB_Spombe positive regulation of septation initiation signaling cascade Traceable author statement. Source: GeneDB_Spombe regulation of G2/M transition of mitotic cell cycle Inferred from mutant phenotype. 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 component	condensed chromosome kinetochore Inferred from direct assay. Source: GeneDB_Spombe medial cortex 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 function	protein binding Inferred from physical interaction. Source: IntAct protein phosphatase inhibitor activity Inferred from genetic interaction. Source: GeneDB_Spombe 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
rad24	P42656	3	EBI-704737,EBI-704791

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 537	537	Tyrosine-protein phosphatase CDC14 homolog		PRO_0000094874
Sites
	Active site	286	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	453	1	Phosphothreonine Ref.3
	Modified residue	468	1	Phosphoserine Ref.3
	Modified residue	470	1	Phosphoserine Ref.3
	Modified residue	513	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9P7H1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F5E50A8C0924C7EA	FASTA	537	60,253
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 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: 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB76271.1.
PIR	T50099.
RefSeq	NP_594716.1. NM_001020143.1.
3D structure databases
ProteinModelPortal	Q9P7H1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P7H1. 4 interactions.
STRING	Q9P7H1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1782.09c.1; SPAC1782.09c.1:pep; SPAC1782.09c.
GeneID	2542358.
GenomeReviews	Gene locus clp1 in contig CU329670_GR.
KEGG	spo:SPAC1782.09c.
NMPDR	fig|4896.1.peg.4686.
Organism-specific databases
GeneDB_Spombe	SPAC1782.09c.
Phylogenomic databases
eggNOG	fuNOG04637.
GeneTree	EFGT00050000004736.
HOGENOM	HBG398632.
OMA	NDDETRT.
OrthoDB	EOG4MD17S.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002796-MONOMER.
Gene expression databases
ArrayExpress	Q9P7H1.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR000387. Tyr/Dual-specificity_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
KO	K06639.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FLP1_SCHPO

Accession

Primary (citable) accession number: Q9P7H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program