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O13453 (PMP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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:
Tyrosine-protein phosphatase pmp1

EC=3.1.3.48
Gene names
Name:pmp1
ORF Names:SPBC1685.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Dual specificity phosphatase that dephosphorylates MAP kinase pmk1 on a Tyr. Has a role in chloride ion homeostasis by inactivating this pmk1 MAP kinase pathway. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Ontologies

Keywords
   Biological processCell cycle
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular chloride ion homeostasis

Inferred from mutant phenotype Ref.1. Source: PomBase

cellular response to salt stress

Inferred from mutant phenotype Ref.1. Source: PomBase

inactivation of MAPK activity

Inferred from direct assay Ref.1. Source: GOC

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.1. Source: PomBase

peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity

Inferred from direct assay Ref.1. Source: GOC

positive regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 12172965. Source: PomBase

protein dephosphorylation

Inferred from direct assay Ref.1. Source: PomBase

regulation of cell morphogenesis

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of cytokinesis

Inferred from mutant phenotype Ref.1. Source: PomBase

regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 12172965. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16291757. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

   Molecular_functionMAP kinase tyrosine phosphatase activity

Inferred from direct assay Ref.1. Source: PomBase

MAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Tyrosine-protein phosphatase pmp1
PRO_0000094917

Sites

Active site1581Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O13453 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0EA71219ED32483F

FASTA27831,628
        10         20         30         40         50         60 
MSQKLPPLKI YTSQLPLVSH KNMLENEEEA SHSQLFTPCP VPPSFPKASK PNSNQPYPNG 

        70         80         90        100        110        120 
PVCIYPPNIY LYAKPTMPII QSFDVVINVA KEVLHPFRTD GRHYRDSKHN LDIQVFDHIE 

       130        140        150        160        170        180 
YVHIHWDHDT QFALELDKLV SFVAYNAMQL NKKVLINCQM GISRSACLMI AFIMKTLNLN 

       190        200        210        220        230        240 
VSDAYEYVKE RSPWIGPNMS LIFQLSEYQQ IIRKNSSQGP YQSSSLKQSK RKSEGNLLFP 

       250        260        270 
EKPHSAQLPL VSPSTSESSM FTNLRRTRSS GSISNDAS 

« Hide

References

« Hide 'large scale' references
[1]"pmp1+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast."
Sugiura R., Toda T., Shuntoh H., Yanagida M., Kuno T.
EMBO J. 17:140-148(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D82022 Genomic DNA. Translation: BAA22897.1.
CU329671 Genomic DNA. Translation: CAA20049.1.
PIRT39517.
RefSeqNP_595205.1. NM_001021111.2.

3D structure databases

ProteinModelPortalO13453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276563. 89 interactions.
MINTMINT-4666651.
STRING4896.SPBC1685.01-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1685.01.1; SPBC1685.01.1:pep; SPBC1685.01.
GeneID2540019.
KEGGspo:SPBC1685.01.

Organism-specific databases

PomBaseSPBC1685.01.

Phylogenomic databases

eggNOGCOG2453.
KOK11240.
OrthoDBEOG7HF1WG.
PhylomeDBO13453.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801162.

Entry information

Entry namePMP1_SCHPO
AccessionPrimary (citable) accession number: O13453
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 89 of the entry and version 1 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