CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006818
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxiredoxin type-2 
Protein Synonyms/Alias
 AHPC1; Cytoplasmic thiol peroxidase 3; cTPx 3; Peroxiredoxin type II; Peroxisomal alkyl hydroperoxide reductase; TPx type II; Thiol-specific antioxidant II; TSA II; Thioredoxin peroxidase type II; Thioredoxin reductase type II 
Gene Name
 AHP1 
Gene Synonyms/Alias
 YLR109W; L2916; L9354.5 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
8MSDLVNKKFPAGDYKubiquitination[1]
32DADSESCKMPQTVEWacetylation[2]
32DADSESCKMPQTVEWubiquitination[1]
41PQTVEWSKLISENKKacetylation[2]
48KLISENKKVIITGAPubiquitination[1, 3]
102FANQAWAKSLGVKDTubiquitination[1]
107WAKSLGVKDTTHIKFacetylation[2]
107WAKSLGVKDTTHIKFubiquitination[1]
113VKDTTHIKFASDPGCacetylation[2]
113VKDTTHIKFASDPGCubiquitination[1, 3]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H(2)O(2). Involved in cellular Mn(2+) homeostasis. 
Sequence Annotation
 DOMAIN 9 176 Thioredoxin.
 ACT_SITE 62 62 Cysteine sulfenic acid (-SOH)
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 116 116 Phosphoserine.
 DISULFID 62 62 Interchain (with C-120); in linked form.
 DISULFID 120 120 Interchain (with C-62); in linked form.  
Keyword
 3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 176 AA 
Protein Sequence
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP 60
TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC 120
AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL 176 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
 GO:0045454; P:cell redox homeostasis; IMP:SGD.
 GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
 GO:0010038; P:response to metal ion; IMP:SGD. 
Interpro
 IPR013740; Redoxin.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF08534; Redoxin 
SMART
  
PROSITE
 PS51352; THIOREDOXIN_2 
PRINTS