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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • GDP-dissociation inhibitor activity Source: SGD
  • G-protein alpha-subunit binding Source: SGD
  • signal transducer activity Source: SGD

GO - Biological processi

  • glucose mediated signaling pathway Source: SGD
  • G-protein coupled receptor signaling pathway Source: SGD
  • invasive growth in response to glucose limitation Source: SGD
  • negative regulation of translation Source: SGD
  • negative regulation of translational frameshifting Source: SGD
  • regulation of catalytic activity Source: GOC
Complete GO annotation...

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 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR116C.
SGDiS000004722. ASC1.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
Complete GO annotation...

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi35292. 276 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 – 139Combined sources
Beta strandi20 – 256Combined sources
Beta strandi32 – 376Combined sources
Beta strandi40 – 5011Combined sources
Beta strandi53 – 6210Combined sources
Beta strandi68 – 736Combined sources
Beta strandi77 – 848Combined sources
Beta strandi87 – 937Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi168 – 1736Combined sources
Beta strandi178 – 1825Combined sources
Turni183 – 1864Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi208 – 2158Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2246Combined sources
Turni225 – 2284Combined sources
Beta strandi229 – 2357Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi247 – 25610Combined sources
Beta strandi259 – 2646Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2746Combined sources
Helixi283 – 2853Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi298 – 3058Combined sources
Beta strandi310 – 3178Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TRJelectron microscopy11.70A1-314[»]
3FRXX-ray2.13A/B/C/D1-319[»]
3J6Xelectron microscopy6.10RA1-319[»]
3J6Yelectron microscopy6.10RA1-319[»]
3J77electron microscopy6.20RC1-319[»]
3J78electron microscopy6.30RC1-319[»]
3RFGX-ray3.90A/B2-319[»]
3RFHX-ray2.90A/B/C/D2-319[»]
4U3MX-ray3.00SR/sR2-319[»]
4U3NX-ray3.20SR/sR2-319[»]
4U3UX-ray2.90SR/sR2-319[»]
4U4NX-ray3.10SR/sR2-319[»]
4U4OX-ray3.60SR/sR2-319[»]
4U4QX-ray3.00SR/sR2-319[»]
4U4RX-ray2.80SR/sR2-319[»]
4U4UX-ray3.00SR/sR2-319[»]
4U4YX-ray3.20SR/sR2-319[»]
4U4ZX-ray3.10SR/sR2-319[»]
4U50X-ray3.20SR/sR2-319[»]
4U51X-ray3.20SR/sR2-319[»]
4U52X-ray3.00SR/sR2-319[»]
4U53X-ray3.30SR/sR2-319[»]
4U55X-ray3.20SR/sR2-319[»]
4U56X-ray3.45SR/sR2-319[»]
4U6FX-ray3.10SR/sR2-319[»]
4V6Ielectron microscopy8.80Aa1-319[»]
4V7RX-ray4.00AT/CT1-319[»]
4V88X-ray3.00Ag/Cg1-319[»]
4V8Yelectron microscopy4.30A61-319[»]
4V8Zelectron microscopy6.60A61-319[»]
4V92electron microscopy3.70g4-318[»]
ProteinModelPortaliP38011.
SMRiP38011. Positions 1-319.
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.
GeneTreeiENSGT00790000123044.
HOGENOMiHOG000091643.
InParanoidiP38011.
KOiK14753.
OMAiRQFISHT.
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

        10         20         30         40         50
MASNEVLVLR GTLEGHNGWV TSLATSAGQP NLLLSASRDK TLISWKLTGD
60 70 80 90 100
DQKFGVPVRS FKGHSHIVQD CTLTADGAYA LSASWDKTLR LWDVATGETY
110 120 130 140 150
QRFVGHKSDV MSVDIDKKAS MIISGSRDKT IKVWTIKGQC LATLLGHNDW
160 170 180 190 200
VSQVRVVPNE KADDDSVTII SAGNDKMVKA WNLNQFQIEA DFIGHNSNIN
210 220 230 240 250
TLTASPDGTL IASAGKDGEI MLWNLAAKKA MYTLSAQDEV FSLAFSPNRY
260 270 280 290 300
WLAAATATGI KVFSLDPQYL VDDLRPEFAG YSKAAEPHAV SLAWSADGQT
310
LFAGYTDNVI RVWQVMTAN
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TRJelectron microscopy11.70A1-314[»]
3FRXX-ray2.13A/B/C/D1-319[»]
3J6Xelectron microscopy6.10RA1-319[»]
3J6Yelectron microscopy6.10RA1-319[»]
3J77electron microscopy6.20RC1-319[»]
3J78electron microscopy6.30RC1-319[»]
3RFGX-ray3.90A/B2-319[»]
3RFHX-ray2.90A/B/C/D2-319[»]
4U3MX-ray3.00SR/sR2-319[»]
4U3NX-ray3.20SR/sR2-319[»]
4U3UX-ray2.90SR/sR2-319[»]
4U4NX-ray3.10SR/sR2-319[»]
4U4OX-ray3.60SR/sR2-319[»]
4U4QX-ray3.00SR/sR2-319[»]
4U4RX-ray2.80SR/sR2-319[»]
4U4UX-ray3.00SR/sR2-319[»]
4U4YX-ray3.20SR/sR2-319[»]
4U4ZX-ray3.10SR/sR2-319[»]
4U50X-ray3.20SR/sR2-319[»]
4U51X-ray3.20SR/sR2-319[»]
4U52X-ray3.00SR/sR2-319[»]
4U53X-ray3.30SR/sR2-319[»]
4U55X-ray3.20SR/sR2-319[»]
4U56X-ray3.45SR/sR2-319[»]
4U6FX-ray3.10SR/sR2-319[»]
4V6Ielectron microscopy8.80Aa1-319[»]
4V7RX-ray4.00AT/CT1-319[»]
4V88X-ray3.00Ag/Cg1-319[»]
4V8Yelectron microscopy4.30A61-319[»]
4V8Zelectron microscopy6.60A61-319[»]
4V92electron microscopy3.70g4-318[»]
ProteinModelPortaliP38011.
SMRiP38011. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35292. 276 interactions.
DIPiDIP-6465N.
IntActiP38011. 71 interactions.
MINTiMINT-652105.
STRINGi4932.YMR116C.

2D gel databases

UCD-2DPAGEP38011.

Proteomic databases

MaxQBiP38011.
PaxDbiP38011.
PeptideAtlasiP38011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YMR116C.
SGDiS000004722. ASC1.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00790000123044.
HOGENOMiHOG000091643.
InParanoidiP38011.
KOiK14753.
OMAiRQFISHT.
OrthoDBiEOG73Z348.

Enzyme and pathway databases

BioCyciYEAST:G3O-32811-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38011.
NextBioi978537.
PROiP38011.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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: June 24, 2015
This is version 144 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

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 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.