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P40048

- PTP3_YEAST

UniProt

P40048 - PTP3_YEAST

Protein

Tyrosine-protein phosphatase 3

Gene

PTP3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei804 – 8041Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: SGD

    GO - Biological processi

    1. inactivation of MAPK activity involved in conjugation with cellular fusion Source: SGD
    2. inactivation of MAPK activity involved in osmosensory signaling pathway Source: SGD
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. protein dephosphorylation Source: SGD
    5. regulation of protein localization Source: SGD
    6. regulation of sporulation Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30246-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase 3 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase 3
    Short name:
    PTPase 3
    Gene namesi
    Name:PTP3
    Ordered Locus Names:YER075C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER075c.
    SGDiS000000877. PTP3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 928928Tyrosine-protein phosphatase 3PRO_0000094857Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphothreonine2 Publications
    Modified residuei248 – 2481Phosphoserine1 Publication
    Modified residuei297 – 2971Phosphoserine1 Publication
    Modified residuei368 – 3681Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40048.
    PaxDbiP40048.
    PeptideAtlasiP40048.

    Expressioni

    Gene expression databases

    GenevestigatoriP40048.

    Interactioni

    Subunit structurei

    Interacts with HOG1.1 Publication

    Protein-protein interaction databases

    BioGridi36819. 79 interactions.
    DIPiDIP-2370N.
    IntActiP40048. 2 interactions.
    MINTiMINT-376861.
    STRINGi4932.YER075C.

    Structurei

    3D structure databases

    ProteinModelPortaliP40048.
    SMRiP40048. Positions 529-877.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 232122RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini502 – 878377Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi308 – 3114Poly-Ser
    Compositional biasi592 – 5976Poly-Thr
    Compositional biasi702 – 71514Poly-AsnAdd
    BLAST
    Compositional biasi724 – 7329Poly-Asp

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00690000103379.
    HOGENOMiHOG000115788.
    KOiK01104.
    OMAiLFKFQLP.
    OrthoDBiEOG7CVQ79.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 2 hits.
    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. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    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.

    P40048-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDSVDCPSI LPTDRTSVLS ETSTLVGSSS HVYSRHAPMN SYHNSMNSNI    50
    YHSPKASSPL VSYKTSSPVL LKRATAPVLP SFKPKEQRYN KPQGCSLITA 100
    VELGKIIETL PDEKVLLLDV RPFTEHAKSI ITNSIHVCLP STLLRRKNFT 150
    FSKLLDNLTP SEQSVLKSKL AIDNLRIIIY DSTANQTESS VSLPCYGIAS 200
    KLIEFDTNVK KTVSILMCGF PQFKILFPDH INTNTFNSDC ISSAEPKSPK 250
    TNLMNSLHNT APHMTATTPL SSPQMNLKLK VPDDSRSDHS NFSSSPSPRN 300
    VLSDSPMSSS SPISALFKFQ LPAPQTNINQ MFKFSQNEEI MGLETYLSAV 350
    NIKEEHERWY NNDSAKKSLQ NFQFPKNQNS LEKDTNKDKL GFQIRYENLS 400
    KNYEKEVIDS VIPEWFQHLM SIPKIELVSQ FQKLDFLEKR RLNHSVSFRK 450
    KENSFILEKP SSYPEQLTST SSSTIMPPKF PDVNKVQKRS HSQPIFTQYS 500
    KYKSMLSLES DSDSESDDVI ISSGVELGAK NRYKDIFPYE HSRVILKKGL 550
    QSSKGIKHSH STSDGGILDN YINANYLSLP RFSVEQNSSF QTTTTTTRRV 600
    RYIATQAPMP STVHDFYTCI LNNGVPLVLS LTNDFENGIE KCYRYWQEGN 650
    YNGIHVKLLE KKILKMPSTT SMRKNTMGTQ NSSLYSAGVQ GNSSNYSTDN 700
    DNDNDNNNNN NNNSNIAVTA AACDDDDDDD DDAILIRKIL LTYHDQEKPY 750
    ELLQIQVKNW PDLGTLLNPI SILQAINVKN HIIDTLFARN YYQNDQLPTI 800
    LVHCSAGCGR TGTLCTIDSI LSNFEMFEML QKEFVKLKYP AKLFDPISWT 850
    INIFRKQRIS MVQNINQFIF IYDCLLFYFR LRLDDITERT DGDGSNKDNI 900
    SLSALIEQIE KLEILQTFVD DKLKELPQ 928
    Length:928
    Mass (Da):105,224
    Last modified:September 21, 2011 - v2
    Checksum:i9BB710EDAF7E3940
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti717 – 7171A → P in AAB70811. (PubMed:9224718)Curated
    Sequence conflicti717 – 7171A → P in AAB64614. (PubMed:9169868)Curated
    Sequence conflicti738 – 7381K → Q in AAB70811. (PubMed:9224718)Curated
    Sequence conflicti738 – 7381K → Q in AAB64614. (PubMed:9169868)Curated
    Sequence conflicti857 – 8571Q → E in AAB70811. (PubMed:9224718)Curated
    Sequence conflicti857 – 8571Q → E in AAB64614. (PubMed:9169868)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006304 Genomic DNA. Translation: AAB70811.1.
    U18814 Genomic DNA. Translation: AAB64614.1.
    BK006939 Genomic DNA. Translation: DAA07735.2.
    PIRiS50578.
    RefSeqiNP_010998.2. NM_001178966.2.

    Genome annotation databases

    EnsemblFungiiYER075C; YER075C; YER075C.
    GeneIDi856807.
    KEGGisce:YER075C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006304 Genomic DNA. Translation: AAB70811.1 .
    U18814 Genomic DNA. Translation: AAB64614.1 .
    BK006939 Genomic DNA. Translation: DAA07735.2 .
    PIRi S50578.
    RefSeqi NP_010998.2. NM_001178966.2.

    3D structure databases

    ProteinModelPortali P40048.
    SMRi P40048. Positions 529-877.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36819. 79 interactions.
    DIPi DIP-2370N.
    IntActi P40048. 2 interactions.
    MINTi MINT-376861.
    STRINGi 4932.YER075C.

    Proteomic databases

    MaxQBi P40048.
    PaxDbi P40048.
    PeptideAtlasi P40048.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER075C ; YER075C ; YER075C .
    GeneIDi 856807.
    KEGGi sce:YER075C.

    Organism-specific databases

    CYGDi YER075c.
    SGDi S000000877. PTP3.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00690000103379.
    HOGENOMi HOG000115788.
    KOi K01104.
    OMAi LFKFQLP.
    OrthoDBi EOG7CVQ79.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30246-MONOMER.

    Miscellaneous databases

    NextBioi 983065.

    Gene expression databases

    Genevestigatori P40048.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 2 hits.
    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. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    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

    1. "Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae."
      Zhan X.-L., Deschenes R.J., Guan K.-L.
      Genes Dev. 11:1690-1702(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 717; 738 AND 857.
      Strain: ATCC 204508 / S288c.
    4. "Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases."
      Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.
      Mol. Cell. Biol. 17:1289-1297(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1."
      Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.
      J. Biol. Chem. 272:17749-17755(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HOG1.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-297 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPTP3_YEAST
    AccessioniPrimary (citable) accession number: P40048
    Secondary accession number(s): D3DLY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 768 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3