P13681 (PP11_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-1
EC=3.1.3.16

Gene names

Name:	dis2
Synonyms:	bws1
ORF Names:	SPBC776.02c

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	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis.
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	Oligomer.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from genetic interaction PubMed 14765108. Source: PomBase attachment of spindle microtubules to kinetochore involved in mitotic sister chromatid segregation Inferred from genetic interaction PubMed 21965289. Source: PomBase cell division Inferred from electronic annotation. Source: UniProtKB-KW protein dephosphorylation Inferred from direct assay PubMed 14765108. Source: PomBase rRNA processing Inferred from sequence orthology. Source: PomBase regulation of homologous chromosome segregation Inferred from mutant phenotype Ref.2. Source: PomBase regulation of mitotic sister chromatid segregation Inferred from mutant phenotype PubMed 3409871. Source: PomBase signal transduction Non-traceable author statement. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay PubMed 14617822. Source: PomBase protein phosphatase type 1 complex Inferred from sequence orthology Ref.2. Source: PomBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.4. Source: PomBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tea4	O60132	2	EBI-4320127,EBI-1099982

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 327	327	Serine/threonine-protein phosphatase PP1-1		PRO_0000058818
Sites
	Active site	124	1	Proton donor By similarity
	Metal binding	63	1	Iron By similarity
	Metal binding	65	1	Iron By similarity
	Metal binding	91	1	Iron By similarity
	Metal binding	91	1	Manganese By similarity
	Metal binding	123	1	Manganese By similarity
	Metal binding	172	1	Manganese By similarity
	Metal binding	247	1	Manganese By similarity
Amino acid modifications
	Modified residue	316	1	Phosphothreonine; by CDC2
Experimental info
	Mutagenesis	245	1	R → Q: Cold-sensitive phenotype.
	Sequence conflict	17	1	E → EGE Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P13681 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 1106BB9C7D6FDCFB	FASTA	327	37,636
	10 20 30 40 50 60 MSNPDVDLDS IIDRLLEVRG SRPGRQVQLS EDEIRFLCNK AREIFISQPI LLELEAPLKI 70 80 90 100 110 120 CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL EVICLLLAYK IKYPENFFIL 130 140 150 160 170 180 RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN 190 200 210 220 230 240 SMDQIQRIMR PTDVPDTGLL CDLLWSDPDK DLTGWGDNDR GVSFTFGPDV VSRFLHKHDM 250 260 270 280 290 300 DLVCRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK 310 320 KQRYGYQGSS QNWHMTPPRK NKTGNSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of a type 1 protein phosphatase encoded by bws1+ in fission yeast mitotic control." Booher R., Beach D. Cell 57:1009-1016(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SP557.
[2]	"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases." Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M. Cell 57:997-1007(1989) [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]	"Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle." Kinoshita N., Ohkura H., Yanagida M. Cell 63:405-415(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTANT CS. Strain: 972 / HM123.
[5]	"Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regulation." Yamano H., Ishii K., Yanagida M. EMBO J. 13:5310-5318(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27075 Genomic DNA. Translation: AAA74731.1. M27068 Genomic DNA. Translation: AAA89197.1. CU329671 Genomic DNA. Translation: CAA22875.1.
PIR	A32550.
RefSeq	NP_596317.1. NM_001022239.2.
3D structure databases
ProteinModelPortal	P13681.
SMR	P13681. Positions 1-308.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13681. 2 interactions.
MINT	MINT-4687271.
STRING	4896.SPBC776.02c-1.
Proteomic databases
PaxDb	P13681.
PRIDE	P13681.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC776.02c.1; SPBC776.02c.1:pep; SPBC776.02c.
GeneID	2541193.
KEGG	spo:SPBC776.02c.
Organism-specific databases
PomBase	SPBC776.02c.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172697.
KO	K06269.
OMA	APNYCNE.
OrthoDB	EOG4MGWH2.
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	20802305.

Entry information

Entry name

PP11_SCHPO

Accession

Primary (citable) accession number: P13681

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 29, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program