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P38011

- GBLP_YEAST

UniProt

P38011 - GBLP_YEAST

Protein

Guanine nucleotide-binding protein subunit beta-like protein

Gene

ASC1

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 136 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.1 Publication

    GO - Molecular functioni

    1. GDP-dissociation inhibitor activity Source: SGD
    2. G-protein alpha-subunit binding Source: SGD
    3. signal transducer activity Source: SGD

    GO - Biological processi

    1. glucose mediated signaling pathway Source: SGD
    2. G-protein coupled receptor signaling pathway Source: SGD
    3. invasive growth in response to glucose limitation Source: SGD
    4. negative regulation of translation Source: SGD
    5. regulation of catalytic activity Source: GOC

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32811-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein subunit beta-like protein
    Alternative name(s):
    Receptor for activated C kinase
    Receptor of activated protein kinase C 1
    Short name:
    RACK1
    Gene namesi
    Name:ASC1
    Synonyms:CPC2
    Ordered Locus Names:YMR116C
    ORF Names:YM9718.15C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    SGDiS000004722. ASC1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 319318Guanine nucleotide-binding protein subunit beta-like proteinPRO_0000127758Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei96 – 961Phosphothreonine1 Publication
    Modified residuei168 – 1681Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP38011.
    PaxDbiP38011.
    PeptideAtlasiP38011.

    2D gel databases

    UCD-2DPAGEP38011.

    Expressioni

    Gene expression databases

    GenevestigatoriP38011.

    Interactioni

    Subunit structurei

    Component of the small (40S) ribosomal subunit. Interacts with the mRNA-binding protein SCP160.3 Publications

    Protein-protein interaction databases

    BioGridi35292. 267 interactions.
    DIPiDIP-6465N.
    IntActiP38011. 71 interactions.
    MINTiMINT-652105.
    STRINGi4932.YMR116C.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Beta strandi20 – 256
    Beta strandi32 – 376
    Beta strandi40 – 5011
    Beta strandi53 – 6210
    Beta strandi68 – 736
    Beta strandi77 – 848
    Beta strandi87 – 937
    Turni94 – 974
    Beta strandi98 – 1047
    Beta strandi110 – 1156
    Beta strandi121 – 1266
    Beta strandi131 – 1355
    Beta strandi140 – 1445
    Beta strandi151 – 1566
    Beta strandi168 – 1736
    Beta strandi178 – 1825
    Turni183 – 1864
    Beta strandi187 – 1926
    Beta strandi199 – 2046
    Beta strandi208 – 2158
    Helixi216 – 2183
    Beta strandi219 – 2246
    Turni225 – 2284
    Beta strandi229 – 2357
    Beta strandi240 – 2456
    Beta strandi247 – 25610
    Beta strandi259 – 2646
    Turni265 – 2684
    Beta strandi269 – 2746
    Helixi283 – 2853
    Beta strandi289 – 2946
    Beta strandi298 – 3058
    Beta strandi310 – 3178

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TRJelectron microscopy11.70A1-314[»]
    1VW9electron microscopy6.10h1-319[»]
    1VWVelectron microscopy6.10h1-319[»]
    3FRXX-ray2.13A/B/C/D1-319[»]
    3IZBelectron microscopy-a1-319[»]
    3O2ZX-ray4.00T1-319[»]
    3O30X-ray4.00T1-319[»]
    3RFGX-ray3.90A/B2-319[»]
    3RFHX-ray2.90A/B/C/D2-319[»]
    3U5CX-ray3.00g1-319[»]
    3U5GX-ray3.00g1-319[»]
    4BYLelectron microscopy4.3061-319[»]
    4BYTelectron microscopy6.6061-319[»]
    4CUYelectron microscopy3.70g4-318[»]
    ProteinModelPortaliP38011.
    SMRiP38011. Positions 2-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38011.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati15 – 5541WD 1Add
    BLAST
    Repeati63 – 10240WD 2Add
    BLAST
    Repeati105 – 14541WD 3Add
    BLAST
    Repeati147 – 19145WD 4Add
    BLAST
    Repeati194 – 23340WD 5Add
    BLAST
    Repeati235 – 27541WD 6Add
    BLAST
    Repeati284 – 31936WD 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat G protein beta family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00750000117670.
    HOGENOMiHOG000091643.
    KOiK14753.
    OMAiTVISASW.
    OrthoDBiEOG73Z348.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 6 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P38011-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASNEVLVLR GTLEGHNGWV TSLATSAGQP NLLLSASRDK TLISWKLTGD    50
    DQKFGVPVRS FKGHSHIVQD CTLTADGAYA LSASWDKTLR LWDVATGETY 100
    QRFVGHKSDV MSVDIDKKAS MIISGSRDKT IKVWTIKGQC LATLLGHNDW 150
    VSQVRVVPNE KADDDSVTII SAGNDKMVKA WNLNQFQIEA DFIGHNSNIN 200
    TLTASPDGTL IASAGKDGEI MLWNLAAKKA MYTLSAQDEV FSLAFSPNRY 250
    WLAAATATGI KVFSLDPQYL VDDLRPEFAG YSKAAEPHAV SLAWSADGQT 300
    LFAGYTDNVI RVWQVMTAN 319
    Length:319
    Mass (Da):34,805
    Last modified:January 23, 2007 - v4
    Checksum:iB9A5D4959A3C54FB
    GO

    Sequence cautioni

    The sequence CAA89753.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49702 Genomic DNA. Translation: CAA89753.1. Sequence problems.
    Z49702 Genomic DNA. Translation: CAA89754.1.
    BK006946 Genomic DNA. Translation: DAA10013.1.
    PIRiS54578.
    RefSeqiNP_013834.1. NM_001182616.1.

    Genome annotation databases

    EnsemblFungiiYMR116C; YMR116C; YMR116C.
    GeneIDi855143.
    KEGGisce:YMR116C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49702 Genomic DNA. Translation: CAA89753.1 . Sequence problems.
    Z49702 Genomic DNA. Translation: CAA89754.1 .
    BK006946 Genomic DNA. Translation: DAA10013.1 .
    PIRi S54578.
    RefSeqi NP_013834.1. NM_001182616.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TRJ electron microscopy 11.70 A 1-314 [» ]
    1VW9 electron microscopy 6.10 h 1-319 [» ]
    1VWV electron microscopy 6.10 h 1-319 [» ]
    3FRX X-ray 2.13 A/B/C/D 1-319 [» ]
    3IZB electron microscopy - a 1-319 [» ]
    3O2Z X-ray 4.00 T 1-319 [» ]
    3O30 X-ray 4.00 T 1-319 [» ]
    3RFG X-ray 3.90 A/B 2-319 [» ]
    3RFH X-ray 2.90 A/B/C/D 2-319 [» ]
    3U5C X-ray 3.00 g 1-319 [» ]
    3U5G X-ray 3.00 g 1-319 [» ]
    4BYL electron microscopy 4.30 6 1-319 [» ]
    4BYT electron microscopy 6.60 6 1-319 [» ]
    4CUY electron microscopy 3.70 g 4-318 [» ]
    ProteinModelPortali P38011.
    SMRi P38011. Positions 2-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35292. 267 interactions.
    DIPi DIP-6465N.
    IntActi P38011. 71 interactions.
    MINTi MINT-652105.
    STRINGi 4932.YMR116C.

    2D gel databases

    UCD-2DPAGE P38011.

    Proteomic databases

    MaxQBi P38011.
    PaxDbi P38011.
    PeptideAtlasi P38011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR116C ; YMR116C ; YMR116C .
    GeneIDi 855143.
    KEGGi sce:YMR116C.

    Organism-specific databases

    SGDi S000004722. ASC1.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00750000117670.
    HOGENOMi HOG000091643.
    KOi K14753.
    OMAi TVISASW.
    OrthoDBi EOG73Z348.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32811-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38011.
    NextBioi 978537.
    PROi P38011.

    Gene expression databases

    Genevestigatori P38011.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 6 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Bienvenut W.V., Peters C.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 47-59; 91-102; 138-155; 217-228 AND 262-311, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    4. Cited for: PROTEIN SEQUENCE OF 54-62.
      Strain: ATCC 204508 / S288c.
    5. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
      Norbeck J., Blomberg A.
      J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 63-70 AND 138-149.
      Strain: ATCC 44827 / SKQ2N.
    6. "Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes."
      Baum S., Bittins M., Frey S., Seedorf M.
      Biochem. J. 380:823-830(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 91-102; 162-176; 217-228 AND 250-261, INTERACTION WITH SCP160, SUBUNIT.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression."
      Gerbasi V.R., Weaver C.M., Hill S., Friedman D.B., Link A.J.
      Mol. Cell. Biol. 24:8276-8287(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    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-96, 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: 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 THR-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM."
      Sengupta J., Nilsson J., Gursky R., Spahn C.M., Nissen P., Frank J.
      Nat. Struct. Mol. Biol. 11:957-962(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 1-114, ELECTRON MICROSCOPY, SUBUNIT.

    Entry informationi

    Entry nameiGBLP_YEAST
    AccessioniPrimary (citable) accession number: P38011
    Secondary accession number(s): D6VZT9, Q6LAA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 333112 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3