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Protein

Tyrosine-protein phosphatase pmp1

Gene

pmp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 1581Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: PomBase
  2. MAP kinase tyrosine phosphatase activity Source: PomBase

GO - Biological processi

  1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: GO_Central
  2. cell cycle Source: UniProtKB-KW
  3. cellular chloride ion homeostasis Source: PomBase
  4. cellular response to salt stress Source: PomBase
  5. inactivation of MAPK activity Source: GOC
  6. peptidyl-tyrosine dephosphorylation Source: PomBase
  7. peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: GOC
  8. positive regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: PomBase
  9. protein dephosphorylation Source: PomBase
  10. regulation of cell morphogenesis Source: PomBase
  11. regulation of mitotic cytokinesis Source: PomBase
  12. regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase pmp1 (EC:3.1.3.48)
Gene namesi
Name:pmp1
ORF Names:SPBC1685.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC1685.01.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Tyrosine-protein phosphatase pmp1PRO_0000094917Add
BLAST

Proteomic databases

MaxQBiO13453.

Interactioni

Protein-protein interaction databases

BioGridi276563. 90 interactions.
MINTiMINT-4666651.
STRINGi4896.SPBC1685.01-1.

Structurei

3D structure databases

ProteinModelPortaliO13453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
InParanoidiO13453.
KOiK11240.
OrthoDBiEOG7HF1WG.
PhylomeDBiO13453.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13453-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQKLPPLKI YTSQLPLVSH KNMLENEEEA SHSQLFTPCP VPPSFPKASK
60 70 80 90 100
PNSNQPYPNG PVCIYPPNIY LYAKPTMPII QSFDVVINVA KEVLHPFRTD
110 120 130 140 150
GRHYRDSKHN LDIQVFDHIE YVHIHWDHDT QFALELDKLV SFVAYNAMQL
160 170 180 190 200
NKKVLINCQM GISRSACLMI AFIMKTLNLN VSDAYEYVKE RSPWIGPNMS
210 220 230 240 250
LIFQLSEYQQ IIRKNSSQGP YQSSSLKQSK RKSEGNLLFP EKPHSAQLPL
260 270
VSPSTSESSM FTNLRRTRSS GSISNDAS
Length:278
Mass (Da):31,628
Last modified:January 1, 1998 - v1
Checksum:i0EA71219ED32483F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82022 Genomic DNA. Translation: BAA22897.1.
CU329671 Genomic DNA. Translation: CAA20049.1.
PIRiT39517.
RefSeqiNP_595205.1. NM_001021111.2.

Genome annotation databases

EnsemblFungiiSPBC1685.01.1; SPBC1685.01.1:pep; SPBC1685.01.
GeneIDi2540019.
KEGGispo:SPBC1685.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82022 Genomic DNA. Translation: BAA22897.1.
CU329671 Genomic DNA. Translation: CAA20049.1.
PIRiT39517.
RefSeqiNP_595205.1. NM_001021111.2.

3D structure databases

ProteinModelPortaliO13453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276563. 90 interactions.
MINTiMINT-4666651.
STRINGi4896.SPBC1685.01-1.

Proteomic databases

MaxQBiO13453.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1685.01.1; SPBC1685.01.1:pep; SPBC1685.01.
GeneIDi2540019.
KEGGispo:SPBC1685.01.

Organism-specific databases

PomBaseiSPBC1685.01.

Phylogenomic databases

eggNOGiCOG2453.
InParanoidiO13453.
KOiK11240.
OrthoDBiEOG7HF1WG.
PhylomeDBiO13453.

Miscellaneous databases

NextBioi20801162.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPMP1_SCHPO
AccessioniPrimary (citable) accession number: O13453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: February 4, 2015
This is version 96 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.