P36614 (PPE1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase ppe1
EC=3.1.3.16

Alternative name(s):
Phosphatase esp1

Gene names

Name:	ppe1
Synonyms:	esp1, ppx1
ORF Names:	SPCC1739.12

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. Negatively regulates mis12. Ref.4
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	Interacts with sts5, ekc1 and mis12. Ref.4
Subcellular location	Nucleus. Note: Associated with chromatin. Ref.4
Sequence similarities	Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Mitosis
Cellular component	Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from mutant phenotype PubMed 21680738. Source: PomBase positive regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway Inferred from mutant phenotype PubMed 21680738. Source: PomBase positive regulation of protein dephosphorylation Inferred from mutant phenotype PubMed 21680738. Source: PomBase protein dephosphorylation Inferred by curator. Source: PomBase regulation of cell shape Inferred from mutant phenotype Ref.1. Source: PomBase regulation of chromosome segregation Inferred from mutant phenotype Ref.4. Source: PomBase regulation of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nuclear chromatin Inferred from direct assay Ref.4. Source: PomBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from sequence or structural similarity Ref.1. Source: PomBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ekc1	O74511	2	EBI-1153118,EBI-1153096

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 305	305	Serine/threonine-protein phosphatase ppe1		PRO_0000058882
Sites
	Active site	112	1	Proton donor By similarity
	Metal binding	51	1	Iron By similarity
	Metal binding	53	1	Iron By similarity
	Metal binding	79	1	Iron By similarity
	Metal binding	79	1	Manganese By similarity
	Metal binding	111	1	Manganese By similarity
	Metal binding	161	1	Manganese By similarity
	Metal binding	235	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	P36614 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 001980A1CC7646D7	FASTA	305	35,259
	10 20 30 40 50 60 MFDLDEWIAT VRKCKYLPEH QLKRLCEMVK VILMEESNIQ PVRTPVTVCG DIHGQFYDLL 70 80 90 100 110 120 ELFRVGGELP STNYIFMGDF VDRGYFSLET FTLFMLLKAR YPDKITLLRG NHESRQITQV 130 140 150 160 170 180 YGFYDECQTK YGNANVWKYC CQVFDFLTLA AVIDNKILCV HGGLSPEVRT LDQIRILARA 190 200 210 220 230 240 QEIPHEGSFC DLMWSDPEDI ESWTVSPRGA GWLFGSKVTT EFSQINDLTL IARAHQLVQE 250 260 270 280 290 300 GYKYHFADKN LVTVWSAPNY CYRCGNVASV MKVDESLEPE FRIFSAVADE DRTVPPSRKR SEYFI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the fission yeast protein phosphatase gene ppe1+ involved in cell shape control and mitosis." Shimanuki M., Kinoshita N., Ohkura H., Yoshida T., Toda T., Yanagida M. Mol. Biol. Cell 4:303-313(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / HM123.
[2]	"Interaction of the pim1/spi1 mitotic checkpoint with a protein phosphatase." Matsumoto T., Beach D. Mol. Biol. Cell 4:337-345(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[4]	"The role of Ppe1/PP6 phosphatase for equal chromosome segregation in fission yeast kinetochore." Goshima G., Iwasaki O., Obuse C., Yanagida M. EMBO J. 22:2752-2763(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH STS5; ECK1 AND MIS12, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13712 Genomic DNA. Translation: BAA02865.1. Z18925 Genomic DNA. Translation: CAA79358.1. CU329672 Genomic DNA. Translation: CAA20786.1.
PIR	A47727.
RefSeq	NP_588420.1. NM_001023411.2.
3D structure databases
ProteinModelPortal	P36614.
SMR	P36614. Positions 3-284.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36614. 2 interactions.
STRING	4896.SPCC1739.12-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1739.12.1; SPCC1739.12.1:pep; SPCC1739.12.
GeneID	2538758.
KEGG	spo:SPCC1739.12.
Organism-specific databases
PomBase	SPCC1739.12.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172696.
KO	K15427.
OMA	NKYGNAN.
OrthoDB	EOG48KVKR.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20799942.

Entry information

Entry name

PPE1_SCHPO

Accession

Primary (citable) accession number: P36614

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program