PRDX2
entrez
7001
canonical
uniprot
P32119
canonical
ensembl
ENSG00000167815
resolver
ensp
ENSP00000301522
resolver
genesymbol
HEL-S-2a
resolver
genesymbol
PRDX2
resolver
genesymbol_syn
NKEFB
resolver
genesymbol_syn
PRDX2
resolver
genesymbol_syn
TDPX1
resolver
hgnc
HGNC:9353
resolver
uniprot
A8K0C0
resolver
uniprot
P31945
resolver
uniprot
P32118
resolver
uniprot
P35701
resolver
uniprot
Q6FHG4
resolver
uniprot
Q92763
resolver
uniprot
Q9UC23
resolver
uniprot
V9HW12
resolver
uniprot_entry
PRDX2_HUMAN
resolver
uniprot_entry
V9HW12_HUMAN
resolver
uniprot_sec
A8K0C0
resolver
uniprot_sec
P31945
resolver
uniprot_sec
P32118
resolver
uniprot_sec
P35701
resolver
uniprot_sec
Q6FHG4
resolver
uniprot_sec
Q92763
resolver
uniprot_sec
Q9UC23
resolver
amino_acid_sequence
MASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN
uniprot
proteins
ec_number
1.11.1.24
uniprot
proteins
function
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). {ECO:0000269|PubMed:9497357}.
uniprot
proteins
mass_dalton
21892
uniprot
proteins
mutagenesis
MUTAGEN 196; /note="K->R: Abolishes acetylation."; /evidence="ECO:0000269|PubMed:18606987
uniprot
proteins
post_translational_modification
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:11904290, ECO:0000269|PubMed:12853451}.; PTM: Acetylation increases resistance to transition to high molecular-mass complexes (PubMed:18606987). Deacetylated by HDAC6 which decreases reducing activity (PubMed:18606987). {ECO:0000269|PubMed:18606987}.
uniprot
proteins
protein_family
AhpC/Prx1 subfamily
uniprot
proteins
protein_family
Peroxiredoxin family
uniprot
proteins
pubmed
10873855
uniprot
proteins
pubmed
11904290
uniprot
proteins
pubmed
12853451
uniprot
proteins
pubmed
1286667
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17141802
uniprot
proteins
pubmed
18606987
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27892488
uniprot
proteins
pubmed
8026862
uniprot
proteins
pubmed
8144038
uniprot
proteins
pubmed
8313871
uniprot
proteins
pubmed
8554614
uniprot
proteins
pubmed
9150948
uniprot
proteins
pubmed
9497357
uniprot
proteins
sequence_length
198
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9497357}.
uniprot
proteins