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P25044

- PTP1_YEAST

UniProt

P25044 - PTP1_YEAST

Protein

Tyrosine-protein phosphatase 1

Gene

PTP1

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 124 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    • Comment

    Functioni

    Is not required for vegetative growth.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei252 – 2521Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein tyrosine phosphatase activity Source: SGD

    GO - Biological processi

    1. invasive growth in response to glucose limitation Source: SGD
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. protein dephosphorylation Source: SGD
    4. pseudohyphal growth Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29609-MONOMER.

    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:PTP1
    Ordered Locus Names:YDL230W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL230w.
    SGDiS000002389. PTP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Tyrosine-protein phosphatase 1PRO_0000094855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphoserine; by CLK11 Publication

    Post-translational modificationi

    Activated by phosphorylation at Ser-83.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25044.
    PaxDbiP25044.
    PeptideAtlasiP25044.

    Expressioni

    Gene expression databases

    GenevestigatoriP25044.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-14183,EBI-16219

    Protein-protein interaction databases

    BioGridi31881. 69 interactions.
    DIPiDIP-2765N.
    IntActiP25044. 13 interactions.
    MINTiMINT-490206.
    STRINGi4932.YDL230W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25044.
    SMRiP25044. Positions 18-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 328314Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117606.
    HOGENOMiHOG000243992.
    KOiK01104.
    OMAiNDARNRY.
    OrthoDBiEOG7R573B.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR016277. Non-rcpt_Tyr_Pase_T1_fun.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000938. PTPN1_yeast. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 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.

    P25044-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAPWYIRQ RDTDLLGKFK FIQNQEDGRL REATNGTVNS RWSLGVSIEP    50
    RNDARNRYVN IMPYERNRVH LKTLSGNDYI NASYVKVNVP GQSIEPGYYI 100
    ATQGPTRKTW DQFWQMCYHN CPLDNIVIVM VTPLVEYNRE KCYQYWPRGG 150
    VDDTVRIASK WESPGGANDM TQFPSDLKIE FVNVHKVKDY YTVTDIKLTP 200
    TDPLVGPVKT VHHFYFDLWK DMNKPEEVVP IMELCAHSHS LNSRGNPIIV 250
    HCSAGVGRTG TFIALDHLMH DTLDFKNITE RSRHSDRATE EYTRDLIEQI 300
    VLQLRSQRMK MVQTKDQFLF IYHAAKYLNS LSVNQ 335
    Length:335
    Mass (Da):38,868
    Last modified:May 1, 1992 - v1
    Checksum:i15F71E50694BE562
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64062 Genomic DNA. Translation: AAA34923.1.
    Z74278 Genomic DNA. Translation: CAA98809.1.
    BK006938 Genomic DNA. Translation: DAA11636.1.
    PIRiA39862.
    RefSeqiNP_010051.1. NM_001180290.1.

    Genome annotation databases

    EnsemblFungiiYDL230W; YDL230W; YDL230W.
    GeneIDi851368.
    KEGGisce:YDL230W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64062 Genomic DNA. Translation: AAA34923.1 .
    Z74278 Genomic DNA. Translation: CAA98809.1 .
    BK006938 Genomic DNA. Translation: DAA11636.1 .
    PIRi A39862.
    RefSeqi NP_010051.1. NM_001180290.1.

    3D structure databases

    ProteinModelPortali P25044.
    SMRi P25044. Positions 18-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31881. 69 interactions.
    DIPi DIP-2765N.
    IntActi P25044. 13 interactions.
    MINTi MINT-490206.
    STRINGi 4932.YDL230W.

    Chemistry

    BindingDBi P25044.
    ChEMBLi CHEMBL4452.

    Proteomic databases

    MaxQBi P25044.
    PaxDbi P25044.
    PeptideAtlasi P25044.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL230W ; YDL230W ; YDL230W .
    GeneIDi 851368.
    KEGGi sce:YDL230W.

    Organism-specific databases

    CYGDi YDL230w.
    SGDi S000002389. PTP1.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117606.
    HOGENOMi HOG000243992.
    KOi K01104.
    OMAi NDARNRY.
    OrthoDBi EOG7R573B.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29609-MONOMER.

    Miscellaneous databases

    NextBioi 968486.

    Gene expression databases

    Genevestigatori P25044.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR016277. Non-rcpt_Tyr_Pase_T1_fun.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000938. PTPN1_yeast. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a yeast protein tyrosine phosphatase."
      Guan K., Deschenes R.J., Qiu H., Dixon J.E.
      J. Biol. Chem. 266:12964-12970(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
      Moeslein F.M., Myers M.P., Landreth G.E.
      J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-83.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPTP1_YEAST
    AccessioniPrimary (citable) accession number: P25044
    Secondary accession number(s): D6VRC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2690 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3