CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005828
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxiredoxin-5, mitochondrial 
Protein Synonyms/Alias
 Alu corepressor 1; Antioxidant enzyme B166; AOEB166; Liver tissue 2D-page spot 71B; PLP; Peroxiredoxin V; Prx-V; Peroxisomal antioxidant enzyme; TPx type VI; Thioredoxin peroxidase PMP20; Thioredoxin reductase 
Gene Name
 PRDX5 
Gene Synonyms/Alias
 ACR1; SBBI10 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31VNLAELFKGKKGVLFubiquitination[1]
50AFTPGCSKTHLPGFVubiquitination[1]
Reference
 [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling. 
Sequence Annotation
 DOMAIN 56 214 Thioredoxin.
 MOTIF 212 214 Microbody targeting signal (By
 ACT_SITE 100 100 Cysteine sulfenic acid (-SOH)
 MOD_RES 83 83 N6-acetyllysine.
 DISULFID 100 204 Redox-active.  
Keyword
 3D-structure; Acetylation; Alternative initiation; Alternative splicing; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Polymorphism; Redox-active center; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 214 AA 
Protein Sequence
MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA 60
EALKAKGVQV VACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI 120
FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPNIIS QL 162 
Gene Ontology
 GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0016209; F:antioxidant activity; IDA:UniProtKB.
 GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
 GO:0004601; F:peroxidase activity; IDA:UniProtKB.
 GO:0051920; F:peroxiredoxin activity; IEA:EC.
 GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB.
 GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
 GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB.
 GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
 GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
 GO:0006954; P:inflammatory response; TAS:UniProtKB.
 GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
 GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB.
 GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
 GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB.
 GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB. 
Interpro
 IPR013740; Redoxin.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF08534; Redoxin 
SMART
  
PROSITE
 PS51352; THIOREDOXIN_2 
PRINTS