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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
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
Proteomesi
  • UP000002311 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001277582 – 319Guanine nucleotide-binding protein subunit beta-like proteinAdd BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei96PhosphothreonineCombined sources1
Cross-linki107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei168PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38011.
PRIDEiP38011.
TopDownProteomicsiP38011.

2D gel databases

UCD-2DPAGEP38011.

PTM databases

iPTMnetiP38011.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • G-protein alpha-subunit binding Source: SGD

Protein-protein interaction databases

BioGridi35292. 273 interactors.
DIPiDIP-6465N.
IntActiP38011. 72 interactors.
MINTiMINT-652105.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Beta strandi20 – 25Combined sources6
Beta strandi32 – 37Combined sources6
Beta strandi40 – 50Combined sources11
Beta strandi53 – 62Combined sources10
Beta strandi68 – 73Combined sources6
Beta strandi77 – 84Combined sources8
Beta strandi87 – 93Combined sources7
Turni94 – 97Combined sources4
Beta strandi98 – 104Combined sources7
Beta strandi110 – 115Combined sources6
Beta strandi121 – 126Combined sources6
Beta strandi131 – 135Combined sources5
Beta strandi140 – 144Combined sources5
Beta strandi151 – 156Combined sources6
Beta strandi168 – 173Combined sources6
Beta strandi178 – 182Combined sources5
Turni183 – 186Combined sources4
Beta strandi187 – 192Combined sources6
Beta strandi199 – 204Combined sources6
Beta strandi208 – 215Combined sources8
Helixi216 – 218Combined sources3
Beta strandi219 – 224Combined sources6
Turni225 – 228Combined sources4
Beta strandi229 – 235Combined sources7
Beta strandi240 – 245Combined sources6
Beta strandi247 – 256Combined sources10
Beta strandi259 – 264Combined sources6
Turni265 – 268Combined sources4
Beta strandi269 – 274Combined sources6
Helixi283 – 285Combined sources3
Beta strandi289 – 294Combined sources6
Beta strandi298 – 305Combined sources8
Beta strandi310 – 317Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15SR/sR2-319[»]
5DC3X-ray3.25SR/sR2-319[»]
5FCIX-ray3.40SR/sR2-319[»]
5FCJX-ray3.10SR/sR2-319[»]
5I4LX-ray3.10SR/sR2-319[»]
5JUOelectron microscopy4.00WA1-319[»]
5JUPelectron microscopy3.50WA1-319[»]
5JUSelectron microscopy4.20WA1-319[»]
5JUTelectron microscopy4.00WA1-319[»]
5JUUelectron microscopy4.00WA1-319[»]
ProteinModelPortaliP38011.
SMRiP38011.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38011.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati15 – 55WD 1Add BLAST41
Repeati63 – 102WD 2Add BLAST40
Repeati105 – 145WD 3Add BLAST41
Repeati147 – 191WD 4Add BLAST45
Repeati194 – 233WD 5Add BLAST40
Repeati235 – 275WD 6Add BLAST41
Repeati284 – 319WD 7Add BLAST36

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

GeneTreeiENSGT00840000129847.
HOGENOMiHOG000091643.
InParanoidiP38011.
KOiK14753.
OMAiNTIGECM.
OrthoDBiEOG092C10HM.

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 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
PDB 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[»]
5DATX-ray3.15SR/sR2-319[»]
5DC3X-ray3.25SR/sR2-319[»]
5FCIX-ray3.40SR/sR2-319[»]
5FCJX-ray3.10SR/sR2-319[»]
5I4LX-ray3.10SR/sR2-319[»]
5JUOelectron microscopy4.00WA1-319[»]
5JUPelectron microscopy3.50WA1-319[»]
5JUSelectron microscopy4.20WA1-319[»]
5JUTelectron microscopy4.00WA1-319[»]
5JUUelectron microscopy4.00WA1-319[»]
ProteinModelPortaliP38011.
SMRiP38011.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35292. 273 interactors.
DIPiDIP-6465N.
IntActiP38011. 72 interactors.
MINTiMINT-652105.

PTM databases

iPTMnetiP38011.

2D gel databases

UCD-2DPAGEP38011.

Proteomic databases

MaxQBiP38011.
PRIDEiP38011.
TopDownProteomicsiP38011.

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

GeneTreeiENSGT00840000129847.
HOGENOMiHOG000091643.
InParanoidiP38011.
KOiK14753.
OMAiNTIGECM.
OrthoDBiEOG092C10HM.

Enzyme and pathway databases

BioCyciYEAST:G3O-32811-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38011.
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...

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: November 30, 2016
This is version 160 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

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 one 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.