Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proteasome component C5  

UniProtKB / Swiss-Prot ID :  PSB1_YEAST

Gene Name (Synonyms) : 
PRE7, PRS3, PTS1 YBL041WYBL0407  

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

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. 

Protein Sequence MATIASEYSSEASNTPIEHQFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIV...
Predicted Secondary Structure CCCCCCEECCCCCCCHHHHHHHHHHHCCCEEEEEEECCEEEEEECCCCCCCCEEECCCCCCEEEECCEEE...
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
53PhosphoserineITDYSINSR
CCCCEEECC
20.36SysPTM
Link
53Phosphoserine.ITDYSINSR
CCCCEEECC
20.36UniProtKB
Link
209PhosphoserineDSFTSATER
HHHHHHHHH
31.05SysPTM
Link
209Phosphoserine.DSFTSATER
HHHHHHHHH
31.05UniProtKB
Link
211PhosphothreonineFTSATERHI
HHHHHHHCC
33.06SysPTM
Link
211Phosphothreonine.FTSATERHI
HHHHHHHCC
33.06UniProtKB
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
"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 SER-209 AND THR-211, 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-53, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures