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P23287

- PP2B1_YEAST

UniProt

P23287 - PP2B1_YEAST

Protein

Serine/threonine-protein phosphatase 2B catalytic subunit A1

Gene

CNA1

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 135 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 1 Fe3+ ion per subunit.By similarity
    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi119 – 1191IronBy similarity
    Metal bindingi121 – 1211IronBy similarity
    Metal bindingi147 – 1471IronBy similarity
    Metal bindingi147 – 1471ZincBy similarity
    Metal bindingi179 – 1791ZincBy similarity
    Active sitei180 – 1801Proton donorBy similarity
    Metal bindingi228 – 2281ZincBy similarity
    Metal bindingi317 – 3171ZincBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: SGD
    2. cellular ion homeostasis Source: SGD
    3. dephosphorylation Source: GOC
    4. fungal-type cell wall organization Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calmodulin-binding, Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32491-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC:3.1.3.16)
    Alternative name(s):
    Calcineurin A1
    Calmodulin-binding protein 1
    Gene namesi
    Name:CNA1
    Synonyms:CMP1
    Ordered Locus Names:YLR433C
    ORF Names:L9753.6
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR433c.
    SGDiS000004425. CNA1.

    Subcellular locationi

    GO - Cellular componenti

    1. calcineurin complex Source: SGD
    2. cytoplasm Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 553552Serine/threonine-protein phosphatase 2B catalytic subunit A1PRO_0000058836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP23287.
    PaxDbiP23287.
    PeptideAtlasiP23287.

    Expressioni

    Gene expression databases

    GenevestigatoriP23287.

    Interactioni

    Subunit structurei

    Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CMD1P067873EBI-12771,EBI-3976

    Protein-protein interaction databases

    BioGridi31692. 65 interactions.
    DIPiDIP-662N.
    IntActiP23287. 23 interactions.
    MINTiMINT-397444.
    STRINGi4932.YLR433C.

    Structurei

    Secondary structure

    1
    553
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi455 – 4584
    Helixi460 – 47415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LHINMR-A453-476[»]
    ProteinModelPortaliP23287.
    SMRiP23287. Positions 13-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063087.
    HOGENOMiHOG000172699.
    KOiK04348.
    OMAiHTIQTFE.
    OrthoDBiEOG77M8X9.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 2 hits.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23287-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKDLNSSRI KIIKPNDSYI KVDRKKDLTK YELENGKVIS TKDRPIASVP    50
    AITGKIPSDE EVFDSKTGLP NHSFLREHFF HEGRLSKEQA IKILNMSTVA 100
    LSKEPNLLKL KAPITICGDI HGQYYDLLKL FEVGGDPAEI DYLFLGDYVD 150
    RGAFSFECLI YLYSLKLNNL GRFWMLRGNH ECKHLTSYFT FKNEMLHKYD 200
    MEVYDACCRS FNVLPLAALM NGQYFCVHGG ISPELKSVED VNKINRFREI 250
    PSRGLMCDLL WADPVENYDD ARDGSEFDQS EDEFVPNSLR GCSFAFTFKA 300
    SCKFLKANGL LSIIRAHEAQ DAGYRMYKNN KVTGFPSLIT MFSAPNYLDT 350
    YHNKAAVLKY EENVMNIRQF HMSPHPYWLP DFMDVFTWSL PFVGEKVTSM 400
    LVSILNICSE QELDPESEPK AAEETVKARA NATKETGTPS DEKASSAILE 450
    DETRRKALRN KILAIAKVSR MFSVLREESE KVEYLKTMNA GVLPRGALAR 500
    GTEGLNETLS TFEKARKEDL INEKLPPSLS EVEQEKIKYY EKILKGAEKK 550
    PQL 553
    Length:553
    Mass (Da):63,002
    Last modified:October 1, 1993 - v2
    Checksum:iD5D6F91CC0BD277B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 462PI → SY in strain: S288c / GRF88.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64839 Genomic DNA. Translation: AAA34465.1.
    X66490 Genomic DNA. Translation: CAA47117.1.
    X54963 Genomic DNA. Translation: CAA38711.1.
    U21094 Genomic DNA. Translation: AAB67518.1.
    AY693079 Genomic DNA. Translation: AAT93098.1.
    BK006945 Genomic DNA. Translation: DAA09734.1.
    PIRiS16809.
    RefSeqiNP_013537.1. NM_001182321.1.

    Genome annotation databases

    EnsemblFungiiYLR433C; YLR433C; YLR433C.
    GeneIDi851153.
    KEGGisce:YLR433C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64839 Genomic DNA. Translation: AAA34465.1 .
    X66490 Genomic DNA. Translation: CAA47117.1 .
    X54963 Genomic DNA. Translation: CAA38711.1 .
    U21094 Genomic DNA. Translation: AAB67518.1 .
    AY693079 Genomic DNA. Translation: AAT93098.1 .
    BK006945 Genomic DNA. Translation: DAA09734.1 .
    PIRi S16809.
    RefSeqi NP_013537.1. NM_001182321.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LHI NMR - A 453-476 [» ]
    ProteinModelPortali P23287.
    SMRi P23287. Positions 13-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31692. 65 interactions.
    DIPi DIP-662N.
    IntActi P23287. 23 interactions.
    MINTi MINT-397444.
    STRINGi 4932.YLR433C.

    Proteomic databases

    MaxQBi P23287.
    PaxDbi P23287.
    PeptideAtlasi P23287.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR433C ; YLR433C ; YLR433C .
    GeneIDi 851153.
    KEGGi sce:YLR433C.

    Organism-specific databases

    CYGDi YLR433c.
    SGDi S000004425. CNA1.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000063087.
    HOGENOMi HOG000172699.
    KOi K04348.
    OMAi HTIQTFE.
    OrthoDBi EOG77M8X9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32491-MONOMER.

    Miscellaneous databases

    NextBioi 967933.

    Gene expression databases

    Genevestigatori P23287.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 2 hits.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase."
      Cyert M.S., Kunisawa R., Kaim D., Thorner J.
      Proc. Natl. Acad. Sci. U.S.A. 88:7376-7380(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / GRF88.
    2. "Identification and molecular characterization of the calmodulin-binding subunit gene (CMP1) of protein phosphatase 2B from Saccharomyces cerevisiae. An alpha-factor inducible gene."
      Ye R.R., Bretscher A.
      Eur. J. Biochem. 204:713-723(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 20B-12.
    3. "The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B."
      Liu Y., Ishii S., Tokai M., Tsutsumi H., Ohki O., Akada R., Tanaka K., Tsuchiya E., Fukui S., Miyakawa T.
      Mol. Gen. Genet. 227:52-59(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP2B1_YEAST
    AccessioniPrimary (citable) accession number: P23287
    Secondary accession number(s): D6VZ68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 135 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 7040 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 XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3