Q06830 · PRDX1_HUMAN
- ProteinPeroxiredoxin-1
- GenePRDX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids199 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 H2O2 (PubMed:9497357).
Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Miscellaneous
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Catalytic activity
- [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:35924 = RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:30879 + CHEBI:15377
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 52 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxiredoxin-1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ06830
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_025050 | 62 | in dbSNP:rs34034070 | |||
Sequence: R → G | ||||||
Mutagenesis | 90 | Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 90 | 87% reduction in enzymatic activity. | ||||
Sequence: T → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 265 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000135076 | 2-199 | UniProt | Peroxiredoxin-1 | |||
Sequence: SSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK | |||||||
Modified residue | 7 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 7 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 16 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 27 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 32 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 35 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Disulfide bond | 52 | UniProt | Interchain (with C-173); in linked form | ||||
Sequence: C | |||||||
Modified residue | 90 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 120 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 136 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 173 | UniProt | Interchain (with C-52); in linked form | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 183 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 185 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K |
Post-translational modification
Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.
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.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Induction
Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (PubMed:18172504).
Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).
Interacts with SESN1 and SESN2 (PubMed:15105503).
Interacts with FAM107A (PubMed:21969592).
Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).
Interacts with SESN1 and SESN2 (PubMed:15105503).
Interacts with FAM107A (PubMed:21969592).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q06830 | AR P10275 | 3 | EBI-353193, EBI-608057 | |
BINARY | Q06830 | DPP9 Q86TI2-2 | 3 | EBI-353193, EBI-21529239 | |
BINARY | Q06830 | MAGEB6 Q8N7X4 | 3 | EBI-353193, EBI-6447163 | |
BINARY | Q06830 | PRDX4 Q13162 | 2 | EBI-353193, EBI-2211957 | |
BINARY | Q06830 | PRNP P04156 | 4 | EBI-353193, EBI-977302 | |
BINARY | Q06830 | PTEN P60484 | 7 | EBI-353193, EBI-696162 | |
BINARY | Q06830 | SRXN1 Q9BYN0 | 3 | EBI-353193, EBI-15678820 | |
BINARY | Q06830 | STK4 Q13043 | 11 | EBI-353193, EBI-367376 | |
BINARY | Q06830 | TERF1 P54274 | 2 | EBI-353193, EBI-710997 | |
BINARY | Q06830 | TPT1 P13693 | 4 | EBI-353193, EBI-1783169 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-165 | Thioredoxin | ||||
Sequence: AKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQF | ||||||
Region | 176-199 | Disordered | ||||
Sequence: GWKPGSDTIKPDVQKSKEYFSKQK | ||||||
Compositional bias | 185-199 | Basic and acidic residues | ||||
Sequence: KPDVQKSKEYFSKQK |
Sequence similarities
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length199
- Mass (Da)22,110
- Last updated1994-06-01 v1
- Checksum8F68E56D75BF5304
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MRQ5 | A0A0A0MRQ5_HUMAN | PRDX1 | 97 | ||
A0A0A0MSI0 | A0A0A0MSI0_HUMAN | PRDX1 | 171 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 147 | in Ref. 2 | ||||
Sequence: L → P | ||||||
Sequence conflict | 149-150 | in Ref. 2 | ||||
Sequence: VG → CC | ||||||
Compositional bias | 185-199 | Basic and acidic residues | ||||
Sequence: KPDVQKSKEYFSKQK | ||||||
Sequence conflict | 189 | in Ref. 2 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 191 | in Ref. 2 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X67951 EMBL· GenBank· DDBJ | CAA48137.1 EMBL· GenBank· DDBJ | mRNA | ||
L19184 EMBL· GenBank· DDBJ | AAA50464.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019740 EMBL· GenBank· DDBJ | AAV38545.1 EMBL· GenBank· DDBJ | mRNA | ||
CR407652 EMBL· GenBank· DDBJ | CAG28580.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ297142 EMBL· GenBank· DDBJ | ABB84465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB451262 EMBL· GenBank· DDBJ | BAG70076.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451388 EMBL· GenBank· DDBJ | BAG70202.1 EMBL· GenBank· DDBJ | mRNA | ||
AL451136 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX06975.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06976.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06979.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06982.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007063 EMBL· GenBank· DDBJ | AAH07063.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021683 EMBL· GenBank· DDBJ | AAH21683.1 EMBL· GenBank· DDBJ | mRNA |