Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein phosphatase PP1-1

Gene

dis2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi65 – 651Manganese 1By similarity
Metal bindingi91 – 911Manganese 1By similarity
Metal bindingi91 – 911Manganese 2By similarity
Metal bindingi123 – 1231Manganese 2By similarity
Active sitei124 – 1241Proton donorBy similarity
Metal bindingi172 – 1721Manganese 2By similarity
Metal bindingi247 – 2471Manganese 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: PomBase
  • protein serine/threonine phosphatase activity Source: PomBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic DNA damage checkpoint Source: PomBase
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of chromosome condensation Source: PomBase
  • positive regulation of establishment of cell polarity regulating cell shape Source: PomBase
  • positive regulation of protein localization to cell tip Source: PomBase
  • protein dephosphorylation Source: PomBase
  • rRNA processing Source: PomBase
  • signal transduction Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-1 (EC:3.1.3.16)
Gene namesi
Name:dis2
Synonyms:bws1
ORF Names:SPBC776.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC776.02c.
PomBaseiSPBC776.02c. dis2.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: PomBase
  • cell division site Source: PomBase
  • CENP-A containing chromatin Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • DPS complex Source: PomBase
  • endocytic vesicle Source: PomBase
  • growing cell tip Source: PomBase
  • mRNA cleavage and polyadenylation specificity factor complex Source: PomBase
  • non-growing cell tip Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
  • protein phosphatase type 1 complex Source: PomBase
  • PTW/PP1 phosphatase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi245 – 2451R → Q: Cold-sensitive phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Serine/threonine-protein phosphatase PP1-1PRO_0000058818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161Phosphothreonine; by CDC21 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13681.
PaxDbiP13681.
PRIDEiP13681.

Interactioni

Subunit structurei

Oligomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
tea4O601322EBI-4320127,EBI-1099982

Protein-protein interaction databases

BioGridi277707. 88 interactions.
IntActiP13681. 2 interactions.
MINTiMINT-4687271.

Structurei

3D structure databases

ProteinModelPortaliP13681.
SMRiP13681. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP13681.
KOiK06269.
OMAiQGLETIC.
OrthoDBiEOG79KPQ9.
PhylomeDBiP13681.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNPDVDLDS IIDRLLEVRG SRPGRQVQLS EDEIRFLCNK AREIFISQPI
60 70 80 90 100
LLELEAPLKI CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL
110 120 130 140 150
EVICLLLAYK IKYPENFFIL RGNHECASIN RIYGFYDECK RRYNIKLWKT
160 170 180 190 200
FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN SMDQIQRIMR PTDVPDTGLL
210 220 230 240 250
CDLLWSDPDK DLTGWGDNDR GVSFTFGPDV VSRFLHKHDM DLVCRAHQVV
260 270 280 290 300
EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
310 320
KQRYGYQGSS QNWHMTPPRK NKTGNSK
Length:327
Mass (Da):37,636
Last modified:January 1, 1990 - v1
Checksum:i1106BB9C7D6FDCFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171E → EGE (PubMed:2544298).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27075 Genomic DNA. Translation: AAA74731.1.
M27068 Genomic DNA. Translation: AAA89197.1.
CU329671 Genomic DNA. Translation: CAA22875.1.
PIRiA32550.
RefSeqiNP_596317.1. NM_001022239.2.

Genome annotation databases

EnsemblFungiiSPBC776.02c.1; SPBC776.02c.1:pep; SPBC776.02c.
GeneIDi2541193.
KEGGispo:SPBC776.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27075 Genomic DNA. Translation: AAA74731.1.
M27068 Genomic DNA. Translation: AAA89197.1.
CU329671 Genomic DNA. Translation: CAA22875.1.
PIRiA32550.
RefSeqiNP_596317.1. NM_001022239.2.

3D structure databases

ProteinModelPortaliP13681.
SMRiP13681. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277707. 88 interactions.
IntActiP13681. 2 interactions.
MINTiMINT-4687271.

Proteomic databases

MaxQBiP13681.
PaxDbiP13681.
PRIDEiP13681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC776.02c.1; SPBC776.02c.1:pep; SPBC776.02c.
GeneIDi2541193.
KEGGispo:SPBC776.02c.

Organism-specific databases

EuPathDBiFungiDB:SPBC776.02c.
PomBaseiSPBC776.02c. dis2.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
InParanoidiP13681.
KOiK06269.
OMAiQGLETIC.
OrthoDBiEOG79KPQ9.
PhylomeDBiP13681.

Miscellaneous databases

NextBioi20802305.
PROiP13681.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPP11_SCHPO
AccessioniPrimary (citable) accession number: P13681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 22, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.