Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glutaredoxin-2, mitochondrial  

UniProtKB / Swiss-Prot ID :  GLRX2_YEAST

Gene Name (Synonyms) : 
GRX2, TTR, TTR1 YDR513WD9719.17  

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

Subcellular Localization :  Cytoplasm. Mitochondrion. Note=Two forms, a long and a short one are found in the mitochondrion, but only the short one is detected in the cytoplasm. 

Protein Function :  Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. 

Protein Sequence METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLST...
Predicted Secondary Structure CCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHCCCEEEEECCCCCHHHHHHHH...
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
37PhosphoserinePKMVSQETV
CCCCCHHHH
20.85SysPTM
Link
37Phosphoserine.PKMVSQETV
CCCCCHHHH
20.85UniProtKB
Link
91PhosphoserineLDEMSNGSE
EECCCCCHH
35.67SysPTM
Link
91Phosphoserine.LDEMSNGSE
EECCCCCHH
35.67UniProtKB
Link
94PhosphoserineMSNGSEIQD
CCCCHHHHH
35.46SysPTM
Link
94Phosphoserine.MSNGSEIQD
CCCCHHHHH
35.46UniProtKB
Link
123PhosphoserineIGGNSDLET
ECCHHHHHH
47.01SysPTM
Link
123Phosphoserine.IGGNSDLET
ECCHHHHHH
47.01UniProtKB
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
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-37; SER-91; SER-94 ANDSER-123, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures