Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thioredoxin reductase 1  

UniProtKB / Swiss-Prot ID :  TRXB1_YEAST

Gene Name (Synonyms) : 
TRR1 YDR353W D9476.5  

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

Subcellular Localization :  Cytoplasm. 

Protein Function :  Acts on thioredoxins 1 and 2. 

Protein Sequence MVHNKVTIIGSGPAAHTAAIYLARAEIKPILYEGMMANGIAAGGQLTTTTEIENFPGFPDGLTGSELMDR...
Predicted Secondary Structure CCCEEEEEEECCHHHHHHHHHHHHCCCEEEEEECCCCCCCCCCCEEEEEEHHHHCCCCCCCCCCHHHHHH...
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
11PhosphoserineTIIGSGPAA
EEEECCHHH
31.06SysPTM
Link
11Phosphoserine.TIIGSGPAA
EEEECCHHH
31.06UniProtKB
Link
94PhosphoserineVDLSSKPFK
EEECCCCEE
52.20SysPTM
Link
94Phosphoserine.VDLSSKPFK
EEECCCCEE
52.20UniProtKB
Link
193PhosphothreonineLRASTIMQK
CCHHHHHHH
21.34SysPTM
Link
193Phosphothreonine.LRASTIMQK
CCHHHHHHH
21.34UniProtKB
Link
279PhosphoserineSSLTSVPGF
CEECCCCCE
31.44SysPTM
Link
279Phosphoserine.SSLTSVPGF
CEECCCCCE
31.44UniProtKB
Link
300PhosphoserineQAITSAGSG
HHHHHHHHH
25.23SysPTM
Link
300Phosphoserine.QAITSAGSG
HHHHHHHHH
25.23UniProtKB
Link
303PhosphoserineTSAGSGCMA
HHHHHHHHH
28.65SysPTM
Link
303Phosphoserine.TSAGSGCMA
HHHHHHHHH
28.65UniProtKB
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
"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-11; SER-94; THR-193;SER-279; SER-300 AND SER-303, 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