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P13517

- CAPZB_YEAST

UniProt

P13517 - CAPZB_YEAST

Protein

F-actin-capping protein subunit beta

Gene

CAP2

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 153 (01 Oct 2014)
      Sequence version 3 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. barbed-end actin filament capping Source: SGD
    3. filamentous growth Source: SGD

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31306-MONOMER.
    ReactomeiREACT_189234. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-actin-capping protein subunit beta
    Gene namesi
    Name:CAP2
    Ordered Locus Names:YIL034C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL034c.
    SGDiS000001296. CAP2.

    Subcellular locationi

    Cytoplasmcytoskeletonactin patch 1 Publication. Bud 1 Publication. Bud tip 1 Publication
    Note: Found at cortical actin spots at the site of bud emergence and at the tips of growing buds and shmoos.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. actin filament Source: SGD
    3. cellular bud tip Source: UniProtKB-SubCell
    4. F-actin capping protein complex Source: SGD
    5. WASH complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 287286F-actin-capping protein subunit betaPRO_0000204642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei85 – 851Phosphoserine2 Publications
    Modified residuei92 – 921Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP13517.
    PaxDbiP13517.
    PeptideAtlasiP13517.

    Expressioni

    Gene expression databases

    GenevestigatoriP13517.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAP1P284955EBI-4013,EBI-4003

    Protein-protein interaction databases

    BioGridi34956. 78 interactions.
    DIPiDIP-836N.
    IntActiP13517. 11 interactions.
    MINTiMINT-482123.
    STRINGi4932.YIL034C.

    Structurei

    3D structure databases

    ProteinModelPortaliP13517.
    SMRiP13517. Positions 2-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG291067.
    GeneTreeiENSGT00390000017957.
    HOGENOMiHOG000041208.
    KOiK10365.
    OMAiFDTYREM.
    OrthoDBiEOG78H45S.

    Family and domain databases

    InterProiIPR001698. CapZ_beta.
    IPR019771. F-actin_capping_bsu_CS.
    [Graphical view]
    PANTHERiPTHR10619. PTHR10619. 1 hit.
    PfamiPF01115. F_actin_cap_B. 1 hit.
    [Graphical view]
    PRINTSiPR00192. FACTINCAPB.
    PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13517-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDAQFDAAL DLLRRLNPTT LQENLNNLIE LQPNLAQDLL SSVDVPLSTQ    50
    KDSADSNREY LCCDYNRDID SFRSPWSNTY YPELSPKDLQ DSPFPSAPLR 100
    KLEILANDSF DVYRDLYYEG GISSVYLWDL NEEDFNGHDF AGVVLFKKNQ 150
    SDHSNWDSIH VFEVTTSPSS PDSFNYRVTT TIILHLDKTK TDQNSHMMLS 200
    GNLTRQTEKD IAIDMSRPLD VIFTSHVANL GSLIEDIESQ MRNLLETVYF 250
    EKTRDIFHQT KNAAIASSAE EANKDAQAEV IRGLQSL 287
    Length:287
    Mass (Da):32,629
    Last modified:November 1, 1991 - v3
    Checksum:i6E669023D1378778
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401F → Y in AAA66935. (PubMed:2823100)Curated
    Sequence conflicti146 – 1472FK → I in AAA66935. (PubMed:2823100)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62630 Genomic DNA. Translation: CAA44497.1.
    Z46861 Genomic DNA. Translation: CAA86917.1.
    M17223 Genomic DNA. Translation: AAA66935.1.
    BK006942 Genomic DNA. Translation: DAA08514.1.
    PIRiS49944.
    RefSeqiNP_012230.3. NM_001179384.3.

    Genome annotation databases

    EnsemblFungiiYIL034C; YIL034C; YIL034C.
    GeneIDi854777.
    KEGGisce:YIL034C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62630 Genomic DNA. Translation: CAA44497.1 .
    Z46861 Genomic DNA. Translation: CAA86917.1 .
    M17223 Genomic DNA. Translation: AAA66935.1 .
    BK006942 Genomic DNA. Translation: DAA08514.1 .
    PIRi S49944.
    RefSeqi NP_012230.3. NM_001179384.3.

    3D structure databases

    ProteinModelPortali P13517.
    SMRi P13517. Positions 2-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34956. 78 interactions.
    DIPi DIP-836N.
    IntActi P13517. 11 interactions.
    MINTi MINT-482123.
    STRINGi 4932.YIL034C.

    Proteomic databases

    MaxQBi P13517.
    PaxDbi P13517.
    PeptideAtlasi P13517.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL034C ; YIL034C ; YIL034C .
    GeneIDi 854777.
    KEGGi sce:YIL034C.

    Organism-specific databases

    CYGDi YIL034c.
    SGDi S000001296. CAP2.

    Phylogenomic databases

    eggNOGi NOG291067.
    GeneTreei ENSGT00390000017957.
    HOGENOMi HOG000041208.
    KOi K10365.
    OMAi FDTYREM.
    OrthoDBi EOG78H45S.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31306-MONOMER.
    Reactomei REACT_189234. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    NextBioi 977553.
    PROi P13517.

    Gene expression databases

    Genevestigatori P13517.

    Family and domain databases

    InterProi IPR001698. CapZ_beta.
    IPR019771. F-actin_capping_bsu_CS.
    [Graphical view ]
    PANTHERi PTHR10619. PTHR10619. 1 hit.
    Pfami PF01115. F_actin_cap_B. 1 hit.
    [Graphical view ]
    PRINTSi PR00192. FACTINCAPB.
    PROSITEi PS00231. F_ACTIN_CAPPING_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Disruption of the actin cytoskeleton in yeast capping protein mutants."
      Amatruda J.F., Cannon J.F., Tatchell K., Hug C., Cooper J.A.
      Nature 344:352-354(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Amatruda J.F., Gattermeir D.J., Cooper J.A.
      Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase."
      Cannon J.F., Tatchell K.
      Mol. Cell. Biol. 7:2653-2663(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-195.
    6. "Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein."
      Amatruda J.F., Cooper J.A.
      J. Cell Biol. 117:1067-1076(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 149-156, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    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 SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. 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 nameiCAPZB_YEAST
    AccessioniPrimary (citable) accession number: P13517
    Secondary accession number(s): D6VVP8, Q07082
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6770 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3