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P38011

- GBLP_YEAST

UniProt

P38011 - GBLP_YEAST

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Protein

Guanine nucleotide-binding protein subunit beta-like protein

Gene
ASC1, CPC2, YMR116C, YM9718.15C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  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
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: Chromosome XIII

Organism-specific databases

SGDiS000004722. ASC1.

Subcellular locationi

GO - Cellular componenti

  1. 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 – 11Removed1 Publication
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.

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

Contains 7 WD repeats.

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

« 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].
  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: September 3, 2014
This is version 135 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.

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

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