Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Triosephosphate isomerase  

UniProtKB / Swiss-Prot ID :  TPIS_YEAST

Gene Name (Synonyms) : 
TPI1 YDR050C YD9609.05C  

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

Subcellular Localization :   

Protein Function :   

Protein Sequence MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKA...
Predicted Secondary Structure CCCCCEEEEECCCCCCHHHHHHHHHHHHHCCCCCCCEEEEECCHHHHHHHHHHHCCCCCEEEEECCCCCC...
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
71PhosphoserineYLKASGAFT
CCCCCCCCC
29.12SysPTM
Link
71Phosphoserine.YLKASGAFT
CCCCCCCCC
29.12UniProtKB
Link
96PhosphoserineILGHSERRS
EECCHHHHH
30.88SysPTM
Link
96Phosphoserine.ILGHSERRS
EECCHHHHH
30.88UniProtKB
Link
100PhosphoserineSERRSYFHE
HHHHHHHCC
38.07SysPTM
Link
100Phosphoserine.SERRSYFHE
HHHHHHHCC
38.07UniProtKB
Link
101PhosphotyrosineERRSYFHED
HHHHHHCCC
13.72SysPTM
Link
211PhosphoserineLYGGSANGS
EEECCCCHH
17.75SysPTM
Link
211Phosphoserine.LYGGSANGS
EEECCCCHH
17.75UniProtKB
Link
215PhosphoserineSANGSNAVT
CCCHHHHHH
22.79SysPTM
Link
215Phosphoserine.SANGSNAVT
CCCHHHHHH
22.79UniProtKB
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-96 AND SER-100, AND MASSSPECTROMETRY.
"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-71; SER-211 AND SER-215,AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures