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Protein

CDC25-like phosphatase YCH1

Gene

YCH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protein phosphatase.1 Publication

Kineticsi

  1. KM=3.5 mM for p-nitrophenylphosphate (PNPP)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    GO - Molecular functioni

    • phosphatase activity Source: SGD
    • protein tyrosine phosphatase activity Source: SGD
    • thiosulfate sulfurtransferase activity Source: SGD

    GO - Biological processi

    • dephosphorylation Source: SGD
    • peptidyl-tyrosine dephosphorylation Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30887-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CDC25-like phosphatase YCH1 (EC:3.1.3.-)
    Alternative name(s):
    CDC25 homolog 1
    Gene namesi
    Name:YCH1
    Ordered Locus Names:YGR203W
    ORF Names:G7731
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VII

    Organism-specific databases

    EuPathDBiFungiDB:YGR203W.
    SGDiS000003435. YCH1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 148148CDC25-like phosphatase YCH1PRO_0000202844Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP42937.

    Interactioni

    Protein-protein interaction databases

    BioGridi33456. 28 interactions.
    DIPiDIP-885N.
    IntActiP42937. 8 interactions.
    MINTiMINT-514352.

    Structurei

    Secondary structure

    1
    148
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53Combined sources
    Beta strandi8 – 125Combined sources
    Helixi14 – 2310Combined sources
    Turni27 – 293Combined sources
    Beta strandi33 – 375Combined sources
    Helixi41 – 433Combined sources
    Helixi56 – 616Combined sources
    Helixi63 – 7816Combined sources
    Beta strandi80 – 823Combined sources
    Beta strandi84 – 896Combined sources
    Beta strandi91 – 955Combined sources
    Helixi96 – 10611Combined sources
    Helixi110 – 1134Combined sources
    Beta strandi116 – 1216Combined sources
    Helixi124 – 1329Combined sources
    Turni136 – 1383Combined sources
    Beta strandi139 – 1413Combined sources
    Helixi144 – 1474Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F4AX-ray1.80A/B1-148[»]
    3FS5X-ray1.90A1-148[»]
    ProteinModelPortaliP42937.
    SMRiP42937. Positions 5-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42937.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 137109RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MPI phosphatase family.Curated
    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    InParanoidiP42937.
    KOiK18065.
    OMAiWQEVYGE.
    OrthoDBiEOG76DV56.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42937-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSYSITNVK YLDPTELHRW MQEGHTTTLR EPFQVVDVRG SDYMGGHIKD
    60 70 80 90 100
    GWHYAYSRLK QDPEYLRELK HRLLEKQADG RGALNVIFHC MLSQQRGPSA
    110 120 130 140
    AMLLLRSLDT AELSRCRLWV LRGGFSRWQS VYGDDESVTA GYLPDLWR
    Length:148
    Mass (Da):17,249
    Last modified:November 1, 1995 - v1
    Checksum:i41527DB282CBFF11
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88996.1.
    Z72988 Genomic DNA. Translation: CAA97230.1.
    AY558510 Genomic DNA. Translation: AAS56836.1.
    BK006941 Genomic DNA. Translation: DAA08296.1.
    PIRiS53926.
    RefSeqiNP_011719.1. NM_001181332.1.

    Genome annotation databases

    EnsemblFungiiYGR203W; YGR203W; YGR203W.
    GeneIDi853117.
    KEGGisce:YGR203W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88996.1.
    Z72988 Genomic DNA. Translation: CAA97230.1.
    AY558510 Genomic DNA. Translation: AAS56836.1.
    BK006941 Genomic DNA. Translation: DAA08296.1.
    PIRiS53926.
    RefSeqiNP_011719.1. NM_001181332.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F4AX-ray1.80A/B1-148[»]
    3FS5X-ray1.90A1-148[»]
    ProteinModelPortaliP42937.
    SMRiP42937. Positions 5-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33456. 28 interactions.
    DIPiDIP-885N.
    IntActiP42937. 8 interactions.
    MINTiMINT-514352.

    Proteomic databases

    MaxQBiP42937.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR203W; YGR203W; YGR203W.
    GeneIDi853117.
    KEGGisce:YGR203W.

    Organism-specific databases

    EuPathDBiFungiDB:YGR203W.
    SGDiS000003435. YCH1.

    Phylogenomic databases

    InParanoidiP42937.
    KOiK18065.
    OMAiWQEVYGE.
    OrthoDBiEOG76DV56.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30887-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP42937.
    NextBioi973145.
    PROiP42937.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
      Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
      Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain."
      Hofmann K., Bucher P., Kajava A.V.
      J. Mol. Biol. 282:195-208(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase."
      Moon J., Kim Y.S., Lee J.Y., Cho S.J., Song H.K., Cho J.H., Kim B.M., Kim K.K., Suh S.W.
      Acta Crystallogr. D 56:778-780(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    10. "Crystal structure of Saccharomyces cerevisiae Ygr203w, a homolog of single-domain rhodanese and Cdc25 phosphatase catalytic domain."
      Yeo H.K., Lee J.Y.
      Proteins 76:520-524(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiYCH1_YEAST
    AccessioniPrimary (citable) accession number: P42937
    Secondary accession number(s): D6VUY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: May 11, 2016
    This is version 123 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 2310 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    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 one 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.