Guanine nucleotide-binding protein subunit beta-like protein - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38011 (GBLP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	ASC1
Synonyms:	CPC2
Ordered Locus Names:	YMR116C
ORF Names:	YM9718.15C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.12
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat WD repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from mutant phenotype PubMed 17591772. Source: SGD glucose mediated signaling pathway Inferred from mutant phenotype PubMed 17591772. Source: SGD invasive growth in response to glucose limitation Inferred from mutant phenotype PubMed 17591772. Source: SGD negative regulation of translation Inferred from mutant phenotype Ref.8. Source: SGD
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay Ref.8. Source: SGD
Molecular_function	GDP-dissociation inhibitor activity Inferred from direct assay PubMed 17591772. Source: SGD signal transducer activity Inferred from mutant phenotype PubMed 17591772. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 319

318

Guanine nucleotide-binding protein subunit beta-like protein

PRO_0000127758

Regions

Repeat

15 – 55

WD 1

Repeat

63 – 102

WD 2

Repeat

105 – 145

WD 3

Repeat

147 – 191

WD 4

Repeat

194 – 233

WD 5

Repeat

235 – 275

WD 6

Repeat

284 – 319

WD 7

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

Phosphothreonine Ref.9

Modified residue

Phosphothreonine Ref.9

Modified residue

166

Phosphoserine Ref.10 Ref.11

Modified residue

168

Phosphothreonine Ref.10 Ref.11

Secondary structure

319

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38011 [UniParc].

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

FASTA

319

34,805

        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' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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 AND THR-99, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND THR-168, MASS SPECTROMETRY.
[11]	"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-166 AND THR-168, MASS SPECTROMETRY.
[12]	"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.

PIR

S54578.

RefSeq

NP_013834.1. NM_001182616.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TRJ	electron microscopy	11.70	A	1-314	[»]
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	[»]

ProteinModelPortal

P38011.

SMR

P38011. Positions 2-319.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6465N.

IntAct

P38011. 70 interactions.

MINT

MINT-652105.

STRING

4932.YMR116C.

2D gel databases

UCD-2DPAGE

P38011.

Proteomic databases

PaxDb

P38011.

PeptideAtlas

P38011.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR116C; YMR116C; YMR116C.

GeneID

855143.

KEGG

sce:YMR116C.

Organism-specific databases

SGD

S000004722. ASC1.

Phylogenomic databases

eggNOG

COG2319.

GeneTree

ENSGT00700000104461.

HOGENOM

HOG000091643.

K14753.

OMA

IRVWQVM.

OrthoDB

EOG437VPP.

Gene expression databases

Genevestigator

P38011.

GermOnline

YMR116C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.130.10.10. 2 hits.

InterPro

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]

Pfam

PF00400. WD40. 6 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 7 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38011.

NextBio

978537.

Entry information

Entry name

GBLP_YEAST

Accession

Primary (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:	April 3, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents