Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Guanine nucleotide-binding protein subunit beta-like protein  

UniProtKB / Swiss-Prot ID :  GBLP_YEAST

Gene Name (Synonyms) : 
ASC1, CPC2 YMR116CYM9718.15C  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Cytoplasm. 

Protein 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. 

Protein Sequence MASNEVLVLRGTLEGHNGWVTSLATSAGQPNLLLSASRDKTLISWKLTGDDQKFGVPVRSFKGHSHIVQD...
Predicted Secondary Structure CCCCCCEEEEEEEEECCCCEEEEEEECCCCCEEEEECCCCEEEEEECCCCCEEEEEEEEEEECCCCCEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASNEV
---CCCCCC
22.51UniProtKB
Link
96PhosphothreonineWDVATGETY
EECCCCCEE
35.08SysPTM
Link
96Phosphothreonine.WDVATGETY
EECCCCCEE
35.08UniProtKB
Link
99PhosphothreonineATGETYQRF
CCCCEEEEE
26.71SysPTM
Link
99Phosphothreonine.ATGETYQRF
CCCCEEEEE
26.71UniProtKB
Link
166PhosphoserineADDDSVTII
CCCCCCEEE
28.31SysPTM
Link
166Phosphoserine.ADDDSVTII
CCCCCCEEE
28.31UniProtKB
Link
168PhosphothreonineDDSVTIISA
CCCCEEEEE
19.28SysPTM
Link
168Phosphothreonine.DDSVTIISA
CCCCEEEEE
19.28UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND THR-168, ANDMASS SPECTROMETRY.
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND THR-168, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 AND THR-99, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures