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P32586

- PYP2_SCHPO

UniProt

P32586 - PYP2_SCHPO

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Protein

Tyrosine-protein phosphatase 2

Gene

pyp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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 sitei630 – 6301Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase tyrosine phosphatase activity Source: PomBase
  2. protein tyrosine phosphatase activity Source: PomBase

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  3. negative regulation of stress-activated MAPK cascade Source: PomBase
  4. peptidyl-tyrosine dephosphorylation Source: PomBase
  5. peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: GOC
  6. protein dephosphorylation 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 2 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase 2
Short name:
PTPase 2
Gene namesi
Name:pyp2
ORF Names:SPAC19D5.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC19D5.01.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Tyrosine-protein phosphatase 2PRO_0000094859Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi278675. 58 interactions.
MINTiMINT-4688417.
STRINGi4896.SPAC19D5.01-1.

Structurei

3D structure databases

ProteinModelPortaliP32586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 130110RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini433 – 698266Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5599.
InParanoidiP32586.
KOiK01104.
OrthoDBiEOG7R573B.
PhylomeDBiP32586.

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.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32586-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLHLLSKDEF NSTLKSFEEQ TESVSWIIDL RLHSKYAVSH IKNAINVSLP
60 70 80 90 100
TALLRRPSFD IGKVFACIKC NVKVSLDEIN AIFLYDSSMA GMNRIYDLVQ
110 120 130 140 150
KFRRGGYSKK IYLLSNGFEA FASSHPDAIV STEMVKESVP YKIDINENCK
160 170 180 190 200
LDILHLSDPS AVSTPISPDY SFPLRVPINI PPPLCTPSVV SDTFSEFASH
210 220 230 240 250
AEYPGFSGLT PFSIHSPTAS SVRSCQSIYG SPLSPPNSAF QAEMPYFPIS
260 270 280 290 300
PAISCASSCP STPDEQKNFF IVGNAPQQTP ARPSLRSVPS YPSSNNQRRP
310 320 330 340 350
SASRVRSFSN YVKSSNVVNP SLSQASLEII PRKSMKRDSN AQNDGTSTMT
360 370 380 390 400
SKLKPSVGLS NTRDAPKPGG LRRANKPCFN KETKGSIFSK ENKGPFTCNP
410 420 430 440 450
WGAKKVSPPP CEVLADLNTA SIFYKFKRLE EMEMTRSLAF NDSKSDWCCL
460 470 480 490 500
ASSRSTSISR KNRYTDIVPY DKTRVRLAVP KGCSDYINAS HIDVGNKKYI
510 520 530 540 550
ACQAPKPGTL LDFWEMVWHN SGTNGVIVML TNLYEAGSEK CSQYWPDNKD
560 570 580 590 600
HALCLEGGLR ISVQKYETFE DLKVNTHLFR LDKPNGPPKY IHHFWVHTWF
610 620 630 640 650
DKTHPDIESI TGIIRCIDKV PNDGPMFVHC SAGVGRTGTF IAVDQILQVP
660 670 680 690 700
KNILPKTTNL EDSKDFIFNC VNSLRSQRMK MVQNFEQFKF LYDVVDYLNS
710
GVNQASKPLM T
Length:711
Mass (Da):79,356
Last modified:October 1, 1993 - v1
Checksum:i15A12CDAE13D341E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2755IVGNA → NRRQC in CAA42167. (PubMed:1448087)Curated
Sequence conflicti487 – 4871I → M(PubMed:1668885)Curated
Sequence conflicti515 – 5151E → N(PubMed:1668885)Curated
Sequence conflicti519 – 5191H → D(PubMed:1668885)Curated
Sequence conflicti636 – 6361R → P in CAA42167. (PubMed:1448087)Curated
Sequence conflicti668 – 6703FNC → IQL in CAA42167. (PubMed:1448087)Curated
Sequence conflicti675 – 6762RS → DT in CAA42167. (PubMed:1448087)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S51320 Genomic DNA. Translation: AAB24544.1.
X59599 mRNA. Translation: CAA42167.1.
AB027789 Genomic DNA. Translation: BAA87093.1.
CU329670 Genomic DNA. Translation: CAB16711.1.
PIRiS28391.
T45160.
RefSeqiNP_594899.1. NM_001020328.2.

Genome annotation databases

EnsemblFungiiSPAC19D5.01.1; SPAC19D5.01.1:pep; SPAC19D5.01.
GeneIDi2542200.
KEGGispo:SPAC19D5.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S51320 Genomic DNA. Translation: AAB24544.1 .
X59599 mRNA. Translation: CAA42167.1 .
AB027789 Genomic DNA. Translation: BAA87093.1 .
CU329670 Genomic DNA. Translation: CAB16711.1 .
PIRi S28391.
T45160.
RefSeqi NP_594899.1. NM_001020328.2.

3D structure databases

ProteinModelPortali P32586.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278675. 58 interactions.
MINTi MINT-4688417.
STRINGi 4896.SPAC19D5.01-1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC19D5.01.1 ; SPAC19D5.01.1:pep ; SPAC19D5.01 .
GeneIDi 2542200.
KEGGi spo:SPAC19D5.01.

Organism-specific databases

PomBasei SPAC19D5.01.

Phylogenomic databases

eggNOGi COG5599.
InParanoidi P32586.
KOi K01104.
OrthoDBi EOG7R573B.
PhylomeDBi P32586.

Miscellaneous databases

NextBioi 20803270.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR029021. 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 ]
Pfami PF00581. Rhodanese. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPYP2_SCHPO
AccessioniPrimary (citable) accession number: P32586
Secondary accession number(s): Q9UR59, Q9UU64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 121 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