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P38011 (GBLP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ASC1
Synonyms:CPC2
Ordered Locus Names:YMR116C
ORF Names:YM9718.15C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

Component of the small (40S) ribosomal subunit. Interacts with the mRNA-binding protein SCP160. Ref.6 Ref.8 Ref.14

Subcellular location

Cytoplasm.

Miscellaneous

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

Sequence similarities

Belongs to the WD repeat G protein beta family.

Contains 7 WD repeats.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 319318Guanine nucleotide-binding protein subunit beta-like protein
PRO_0000127758

Regions

Repeat15 – 5541WD 1
Repeat63 – 10240WD 2
Repeat105 – 14541WD 3
Repeat147 – 19145WD 4
Repeat194 – 23340WD 5
Repeat235 – 27541WD 6
Repeat284 – 31936WD 7

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.12
Modified residue961Phosphothreonine Ref.9
Modified residue1681Phosphothreonine Ref.11

Secondary structure

........................................................... 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38011 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: B9A5D4959A3C54FB

FASTA31934,805
        10         20         30         40         50         60 
MASNEVLVLR GTLEGHNGWV TSLATSAGQP NLLLSASRDK TLISWKLTGD DQKFGVPVRS 

        70         80         90        100        110        120 
FKGHSHIVQD CTLTADGAYA LSASWDKTLR LWDVATGETY QRFVGHKSDV MSVDIDKKAS 

       130        140        150        160        170        180 
MIISGSRDKT IKVWTIKGQC LATLLGHNDW VSQVRVVPNE KADDDSVTII SAGNDKMVKA 

       190        200        210        220        230        240 
WNLNQFQIEA DFIGHNSNIN TLTASPDGTL IASAGKDGEI MLWNLAAKKA MYTLSAQDEV 

       250        260        270        280        290        300 
FSLAFSPNRY WLAAATATGI KVFSLDPQYL VDDLRPEFAG YSKAAEPHAV SLAWSADGQT 

       310 
LFAGYTDNVI RVWQVMTAN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49702 Genomic DNA. Translation: CAA89753.1. Sequence problems.
Z49702 Genomic DNA. Translation: CAA89754.1.
BK006946 Genomic DNA. Translation: DAA10013.1.
PIRS54578.
RefSeqNP_013834.1. NM_001182616.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TRJelectron microscopy11.70A1-314[»]
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[»]
ProteinModelPortalP38011.
SMRP38011. Positions 2-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35292. 267 interactions.
DIPDIP-6465N.
IntActP38011. 71 interactions.
MINTMINT-652105.
STRING4932.YMR116C.

2D gel databases

UCD-2DPAGEP38011.

Proteomic databases

MaxQBP38011.
PaxDbP38011.
PeptideAtlasP38011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR116C; YMR116C; YMR116C.
GeneID855143.
KEGGsce:YMR116C.

Organism-specific databases

SGDS000004722. ASC1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00750000117670.
HOGENOMHOG000091643.
KOK14753.
OMATVISASW.
OrthoDBEOG73Z348.

Enzyme and pathway databases

BioCycYEAST:G3O-32811-MONOMER.

Gene expression databases

GenevestigatorP38011.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. 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]
PfamPF00400. WD40. 6 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38011.
NextBio978537.
PROP38011.

Entry information

Entry nameGBLP_YEAST
AccessionPrimary (citable) accession number: P38011
Secondary accession number(s): D6VZT9, Q6LAA5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references