Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peroxiredoxin-5, mitochondrial  

UniProtKB / Swiss-Prot ID :  PRDX5_HUMAN

Gene Name (Synonyms) : 
PRDX5, ACR1 SBBI10  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic+peroxisomal: Cytoplasm. Peroxisome. 

Protein Function :  Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. 

Protein Sequence MGLAGVCALRRSAGYILVGGAGGQSAAAAARRYSEGEWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEG...
Predicted Secondary Structure CCCEEEEEEECCCCCEEECCCCCEEECCCCCCCCCCCEEECCCCCCCCCCCCCCCCCCCCCCCCEEEEEC...
Protein Variant
LocationDescription
33Y -> C (in dbSNP:rs7938623). VAR_025049
157F -> L (in a breast cancer sample;somatic mutation).
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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
Protein Variant
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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
83Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AELFKGKKG
HHHHCCCEE
80.56Phosphositeplus
Link
83N6-acetyllysineAELFKGKKG
HHHHCCCEE
80.56HPRD
Link
83N6-acetyllysineAELFKGKKG
HHHHCCCEE
80.56Phosphositeplus
Link
83N6-acetyllysine.AELFKGKKG
HHHHCCCEE
80.56UniProtKB
Link
97PhosphothreoninePGAFTPGCS
CCCCCCCCC
20.45Phosphositeplus
Link
97PhosphothreoninePGAFTPGCS
CCCCCCCCC
20.45SysPTM
Link
100S-nitrosocysteineFTPGCSKTH
CCCCCCHHH
3.87dbSNO
Link
116N6-acetyllysineAEALKAKGV
HHHHHHCCC
55.91HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CC90B_HUMANphysical interactionEBI-735459
intact16169070
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
TRXR1_HUMANENSP00000265462STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, 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