Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32586 (PYP2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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 2

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 2
Short name=PTPase 2
Gene names
Name:pyp2
ORF Names:SPAC19D5.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Cytoplasm.

Sequence similarities

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

Contains 1 rhodanese domain.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Tyrosine-protein phosphatase 2
PRO_0000094859

Regions

Domain21 – 130110Rhodanese
Domain433 – 698266Tyrosine-protein phosphatase

Sites

Active site6301Phosphocysteine intermediate By similarity

Experimental info

Sequence conflict271 – 2755IVGNA → NRRQC in CAA42167. Ref.2
Sequence conflict4871I → M Ref.5
Sequence conflict5151E → N Ref.5
Sequence conflict5191H → D Ref.5
Sequence conflict6361R → P in CAA42167. Ref.2
Sequence conflict668 – 6703FNC → IQL in CAA42167. Ref.2
Sequence conflict675 – 6762RS → DT in CAA42167. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32586 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 15A12CDAE13D341E

FASTA71179,356
        10         20         30         40         50         60 
MLHLLSKDEF NSTLKSFEEQ TESVSWIIDL RLHSKYAVSH IKNAINVSLP TALLRRPSFD 

        70         80         90        100        110        120 
IGKVFACIKC NVKVSLDEIN AIFLYDSSMA GMNRIYDLVQ KFRRGGYSKK IYLLSNGFEA 

       130        140        150        160        170        180 
FASSHPDAIV STEMVKESVP YKIDINENCK LDILHLSDPS AVSTPISPDY SFPLRVPINI 

       190        200        210        220        230        240 
PPPLCTPSVV SDTFSEFASH AEYPGFSGLT PFSIHSPTAS SVRSCQSIYG SPLSPPNSAF 

       250        260        270        280        290        300 
QAEMPYFPIS PAISCASSCP STPDEQKNFF IVGNAPQQTP ARPSLRSVPS YPSSNNQRRP 

       310        320        330        340        350        360 
SASRVRSFSN YVKSSNVVNP SLSQASLEII PRKSMKRDSN AQNDGTSTMT SKLKPSVGLS 

       370        380        390        400        410        420 
NTRDAPKPGG LRRANKPCFN KETKGSIFSK ENKGPFTCNP WGAKKVSPPP CEVLADLNTA 

       430        440        450        460        470        480 
SIFYKFKRLE EMEMTRSLAF NDSKSDWCCL ASSRSTSISR KNRYTDIVPY DKTRVRLAVP 

       490        500        510        520        530        540 
KGCSDYINAS HIDVGNKKYI ACQAPKPGTL LDFWEMVWHN SGTNGVIVML TNLYEAGSEK 

       550        560        570        580        590        600 
CSQYWPDNKD HALCLEGGLR ISVQKYETFE DLKVNTHLFR LDKPNGPPKY IHHFWVHTWF 

       610        620        630        640        650        660 
DKTHPDIESI TGIIRCIDKV PNDGPMFVHC SAGVGRTGTF IAVDQILQVP KNILPKTTNL 

       670        680        690        700        710 
EDSKDFIFNC VNSLRSQRMK MVQNFEQFKF LYDVVDYLNS GVNQASKPLM T 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine phosphatases that negatively regulate mitosis."
Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L.
Mol. Cell. Biol. 12:5571-5580(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. 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.
[4]"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 285-437.
Strain: ATCC 38364 / 968.
[5]"Protein phosphatases in cell division: how vital are they?"
Yanagida M., Yamano H., Stone E.M., Kinoshita N., Yoshida T., Shiozaki K.
Princess Takamatsu Symp. 22:137-144(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 485-519.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S51320 Genomic DNA. Translation: AAB24544.1.
X59599 mRNA. Translation: CAA42167.1.
AB027789 Genomic DNA. Translation: BAA87093.1.
CU329670 Genomic DNA. Translation: CAB16711.1.
PIRS28391.
T45160.
RefSeqNP_594899.1. NM_001020328.2.

3D structure databases

ProteinModelPortalP32586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278675. 58 interactions.
MINTMINT-4688417.
STRING4896.SPAC19D5.01-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19D5.01.1; SPAC19D5.01.1:pep; SPAC19D5.01.
GeneID2542200.
KEGGspo:SPAC19D5.01.

Organism-specific databases

PomBaseSPAC19D5.01.

Phylogenomic databases

eggNOGCOG5599.
KOK01104.
OrthoDBEOG7R573B.
PhylomeDBP32586.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803270.

Entry information

Entry namePYP2_SCHPO
AccessionPrimary (citable) accession number: P32586
Secondary accession number(s): Q9UR59, Q9UU64
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 116 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