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P06652 (MPIP_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
M-phase inducer phosphatase

EC=3.1.3.48
Alternative name(s):
Mitosis initiation protein
P80
Gene names
Name:cdc25
ORF Names:SPAC24H6.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Sequence caution

The sequence AAA35294.1 differs from that shown. Reason: Frameshift at position 571.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Non-traceable author statement. Source: PomBase

mitotic DNA replication checkpoint

Inferred from mutant phenotype PubMed 1549179. Source: PomBase

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-tyrosine dephosphorylation involved in activation of protein kinase activity

Inferred from direct assay PubMed 1756737. Source: PomBase

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 2665944. Source: PomBase

regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of cell size

Non-traceable author statement. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 1500423. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleus

Inferred from direct assay PubMed 1500423. Source: PomBase

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 1819507PubMed 9774107. Source: PomBase

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 1756737. Source: PomBase

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 1756737PubMed 1819507. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596M-phase inducer phosphatase
PRO_0000198661

Regions

Domain429 – 533105Rhodanese

Sites

Active site4801 By similarity

Amino acid modifications

Modified residue991Phosphoserine Ref.3
Modified residue1781Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
P06652 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: CF8D430FC7BD38C1

FASTA59666,566
        10         20         30         40         50         60 
MDSPLSSLSF TNTLSGKRNV LRPAARELKL MSDRNANQEL DFFFPKSKHI ASTLVDPFGK 

        70         80         90        100        110        120 
TCSTASPASS LAADMSMNMH IDESPALPTP RRTLFRSLSC TVETPLANKT IVSPLPESPS 

       130        140        150        160        170        180 
NDALTESYFF RQPASKYSIT QDSPRVSSTI AYSFKPKASI ALNTTKSEAT RSSLSSSSFD 

       190        200        210        220        230        240 
SYLRPNVSRS RSSGNAPPFL RSRSSSSYSI NKKKGTSGGQ ATRHLTYALS RTCSQSSNTT 

       250        260        270        280        290        300 
SLLESCLTDD TDDFELMSDH EDTFTMGKVA DLPESSVELV EDAASIQRPN SDFGACNDNS 

       310        320        330        340        350        360 
LDDLFQASPI KPIDMLPKIN KDIAFPSLKV RSPSPMAFAM QEDAEYDEQD TPVLRRTQSM 

       370        380        390        400        410        420 
FLNSTRLGLF KSQDLVCVTP KQSTKESERF ISSHVEDLSL PCFAVKEDSL KRITQETLLG 

       430        440        450        460        470        480 
LLDGKFKDIF DKCIIIDCRF EYEYLGGHIS TAVNLNTKQA IVDAFLSKPL THRVALVFHC 

       490        500        510        520        530        540 
EHSAHRAPHL ALHFRNTDRR MNSHRYPFLY YPEVYILHGG YKSFYENHKN RCDPINYVPM 

       550        560        570        580        590 
NDASHVMTCT KAMNNFKRNA TFMRTKSYTF GQSVLASPDV NDSPTAMHSL STLRRF 

« Hide

References

« Hide 'large scale' references
[1]"cdc25+ functions as an inducer in the mitotic control of fission yeast."
Russell P., Nurse P.
Cell 45:145-153(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-178, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13158 Genomic DNA. Translation: AAA35294.1. Frameshift.
CU329670 Genomic DNA. Translation: CAA90849.1.
PIRS62407.
RefSeqNP_592947.1. NM_001018348.2.

3D structure databases

ProteinModelPortalP06652.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279086. 75 interactions.
IntActP06652. 2 interactions.
MINTMINT-4686889.
STRING4896.SPAC24H6.05-1.

Proteomic databases

MaxQBP06652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC24H6.05.1; SPAC24H6.05.1:pep; SPAC24H6.05.
GeneID2542632.
KEGGspo:SPAC24H6.05.

Organism-specific databases

PomBaseSPAC24H6.05.

Phylogenomic databases

eggNOGCOG5105.
KOK02555.
OMAISSHVED.
OrthoDBEOG7VMPGR.
PhylomeDBP06652.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803681.
PROP06652.

Entry information

Entry nameMPIP_SCHPO
AccessionPrimary (citable) accession number: P06652
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names