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Protein

Tyrosine-protein phosphatase 1

Gene

pyp1

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

Plays a role in inhibiting the onset of mitosis. Dephosphorylates sty1/spc1 and wis1/spc2/sty2.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei470 – 4701Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • MAP kinase tyrosine phosphatase activity Source: PomBase
  • protein tyrosine phosphatase activity Source: PomBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  • negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: PomBase
  • negative regulation of transcription by glucose Source: PomBase
  • peptidyl-tyrosine dephosphorylation Source: PomBase
  • peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase 1 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase 1
Short name:
PTPase 1
Gene namesi
Name:pyp1
ORF Names:SPAC26F1.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26F1.10c.
PomBaseiSPAC26F1.10c. pyp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Tyrosine-protein phosphatase 1PRO_0000094858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei320 – 3201Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP27574.

Interactioni

Protein-protein interaction databases

BioGridi279130. 242 interactions.
MINTiMINT-4687977.

Structurei

3D structure databases

ProteinModelPortaliP27574.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini260 – 539280Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5599.
InParanoidiP27574.
KOiK01104.
OMAiCINISTY.
OrthoDBiEOG7JMGNZ.
PhylomeDBiP27574.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFSNGSKSS TFTIAPSGSC IALPPQRGVA TSKYAVHASC LQEYLDKEAW
60 70 80 90 100
KDDTLIIDLR PVSEFSKSRI KGSVNLSLPA TLIKRPAFSV ARIISNLHDV
110 120 130 140 150
DDKRDFQNWQ EFSSILVCVP AWIANYVTNA EVIGEKFRKE SYSGDFGILD
160 170 180 190 200
LDYSKVSGKY PSVIDNSPVK SKLGALPSAR PRLSYSAAQT APISLSSEGS
210 220 230 240 250
DYFSRPPPTP NVAGLSLNNF FCPLPENKDN KSSPFGSATV QTPCLHSVPD
260 270 280 290 300
AFTNPDVATL YQKFLRLQSL EHQRLVSCSD RNSQWSTVDS LSNTSYKKNR
310 320 330 340 350
YTDIVPYNCT RVHLKRTSPS ELDYINASFI KTETSNYIAC QGSISRSISD
360 370 380 390 400
FWHMVWDNVE NIGTIVMLGS LFEAGREMCT AYWPSNGIGD KQVYGDYCVK
410 420 430 440 450
QISEENVDNS RFILRKFEIQ NANFPSVKKV HHYQYPNWSD CNSPENVKSM
460 470 480 490 500
VEFLKYVNNS HGSGNTIVHC SAGVGRTGTF IVLDTILRFP ESKLSGFNPS
510 520 530 540 550
VADSSDVVFQ LVDHIRKQRM KMVQTFTQFK YVYDLIDSLQ KSQVHFPVLT
Length:550
Mass (Da):61,588
Last modified:August 1, 1992 - v1
Checksum:i5DB770AEAAA59F03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63257 mRNA. Translation: AAA35328.1.
CU329670 Genomic DNA. Translation: CAA97367.1.
PIRiA40449.
RefSeqiNP_594885.1. NM_001020314.2.

Genome annotation databases

EnsemblFungiiSPAC26F1.10c.1; SPAC26F1.10c.1:pep; SPAC26F1.10c.
GeneIDi2542677.
KEGGispo:SPAC26F1.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63257 mRNA. Translation: AAA35328.1.
CU329670 Genomic DNA. Translation: CAA97367.1.
PIRiA40449.
RefSeqiNP_594885.1. NM_001020314.2.

3D structure databases

ProteinModelPortaliP27574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279130. 242 interactions.
MINTiMINT-4687977.

Proteomic databases

MaxQBiP27574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26F1.10c.1; SPAC26F1.10c.1:pep; SPAC26F1.10c.
GeneIDi2542677.
KEGGispo:SPAC26F1.10c.

Organism-specific databases

EuPathDBiFungiDB:SPAC26F1.10c.
PomBaseiSPAC26F1.10c. pyp1.

Phylogenomic databases

eggNOGiCOG5599.
InParanoidiP27574.
KOiK01104.
OMAiCINISTY.
OrthoDBiEOG7JMGNZ.
PhylomeDBiP27574.

Miscellaneous databases

NextBioi20803725.
PROiP27574.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases."
    Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L.
    Proc. Natl. Acad. Sci. U.S.A. 88:3455-3459(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
  3. "Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast."
    Millar J.B.A., Russell P., Dixon J.E., Guan K.L.
    EMBO J. 11:4943-4952(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast."
    Millar J.B.A., Buck V., Wilkinson M.G.
    Genes Dev. 9:2117-2130(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPYP1_SCHPO
AccessioniPrimary (citable) accession number: P27574
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 22, 2015
This is version 128 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.