P04040 · CATA_HUMAN
- ProteinCatalase
- GeneCAT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids527 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the degradation of hydrogen peroxide (H2O2) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369).
Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369).
Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369).
Catalytic activity
- 2 H2O2 = 2 H2O + O2
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 75 | |||||
Sequence: H | ||||||
Active site | 148 | |||||
Sequence: N | ||||||
Binding site | 194 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 201 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 203 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 213 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 237 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 303 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 305 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 306 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 358 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Y |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCatalase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP04040
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Acatalasemia (ACATLAS)
- Note
- DescriptionA metabolic disorder characterized by a total or near total loss of catalase activity in red cells. It is often associated with ulcerating oral lesions. Acatalasemia is inherited as an autosomal recessive trait.
- See alsoMIM:614097
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 517-519 | Does not affect localization to peroxisomes. | ||||
Sequence: SHL → TQV | ||||||
Mutagenesis | 524-527 | Abolished localization to peroxisomes. | ||||
Sequence: Missing | ||||||
Mutagenesis | 526 | Abolished localization to peroxisomes. | ||||
Sequence: N → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 630 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000084901 | 2-527 | UniProt | Catalase | |||
Sequence: ADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 221 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 233 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 306 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 306 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 417 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 422 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 480 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 480 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 499 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 511 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 515 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 517 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Homotetramer (PubMed:10656833, PubMed:10666617, PubMed:21976670).
Interacts (via microbody targeting signal) with PEX5, monomeric form interacts with PEX5, leading to its translocation into peroxisomes (PubMed:21976670).
Interacts (via microbody targeting signal) with PEX5, monomeric form interacts with PEX5, leading to its translocation into peroxisomes (PubMed:21976670).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04040 | CAT P04040 | 5 | EBI-2432181, EBI-2432181 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 524-527 | Microbody targeting signal; atypical | ||||
Sequence: KANL |
Sequence similarities
Belongs to the catalase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length527
- Mass (Da)59,756
- Last updated2007-01-23 v3
- Checksum7BAA2394D124ED20
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B3ITJ0 | A0A3B3ITJ0_HUMAN | CAT | 31 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 54 | in Ref. 3; AAK29181 | ||||
Sequence: D → N | ||||||
Sequence conflict | 100 | in Ref. 4; BAG37746 | ||||
Sequence: F → L | ||||||
Sequence conflict | 239 | in Ref. 3; AAK29181 | ||||
Sequence: D → G | ||||||
Sequence conflict | 274 | in Ref. 3; AAK29181 | ||||
Sequence: Y → D | ||||||
Sequence conflict | 301 | in Ref. 3; AAK29181 | ||||
Sequence: K → R | ||||||
Sequence conflict | 366 | in Ref. 4; BAG37746 | ||||
Sequence: L → P | ||||||
Sequence conflict | 449 | in Ref. 4; BAG37746 | ||||
Sequence: N → D | ||||||
Sequence conflict | 514 | in Ref. 3; AAK29181 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 520 | in Ref. 3; AAK29181 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04085 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04086 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04087 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04088 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04089 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04090 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04091 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04092 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04093 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04094 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04095 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04096 EMBL· GenBank· DDBJ | CAA27721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04076 EMBL· GenBank· DDBJ | CAA27717.1 EMBL· GenBank· DDBJ | mRNA | ||
AY028632 EMBL· GenBank· DDBJ | AAK29181.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291585 EMBL· GenBank· DDBJ | BAF84274.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315350 EMBL· GenBank· DDBJ | BAG37746.1 EMBL· GenBank· DDBJ | mRNA | ||
AY545477 EMBL· GenBank· DDBJ | AAS37679.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL035079 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471064 EMBL· GenBank· DDBJ | EAW68170.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68171.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC110398 EMBL· GenBank· DDBJ | AAI10399.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112217 EMBL· GenBank· DDBJ | AAI12218.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112219 EMBL· GenBank· DDBJ | AAI12220.1 EMBL· GenBank· DDBJ | mRNA | ||
L13609 EMBL· GenBank· DDBJ | AAA16651.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K02400 EMBL· GenBank· DDBJ | AAB59522.1 EMBL· GenBank· DDBJ | Genomic DNA |