Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catalase

Gene

CAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.1 Publication

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei751
Active sitei1481
Metal bindingi358Iron (heme axial ligand)1

GO - Molecular functioni

  • aminoacylase activity Source: Ensembl
  • antioxidant activity Source: UniProtKB
  • catalase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: UniProtKB
  • oxidoreductase activity, acting on peroxide as acceptor Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-341.
ZFISH:MONOMER66-341.
BRENDAi1.11.1.6. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-74259. Purine catabolism.
SABIO-RKP04040.
SIGNORiP04040.

Protein family/group databases

PeroxiBasei5282. HsKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:CAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1516. CAT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: Ensembl
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • lysosome Source: Ensembl
  • membrane Source: UniProtKB
  • mitochondrial intermembrane space Source: Ensembl
  • mitochondrion Source: GO_Central
  • peroxisomal matrix Source: Reactome
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Acatalasemia (ACATLAS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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.
See also OMIM:614097

Organism-specific databases

DisGeNETi847.
MalaCardsiCAT.
MIMi614097. phenotype.
OpenTargetsiENSG00000121691.
Orphaneti926. Acatalasemia.
PharmGKBiPA26099.

Chemistry databases

ChEMBLiCHEMBL3627594.
DrugBankiDB01213. Fomepizole.

Polymorphism and mutation databases

BioMutaiCAT.
DMDMi115702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000849012 – 527CatalaseAdd BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei9PhosphoserineCombined sources1
Modified residuei221N6-succinyllysineBy similarity1
Modified residuei233N6-acetyllysineBy similarity1
Modified residuei306N6-acetyllysine; alternateBy similarity1
Modified residuei306N6-succinyllysine; alternateBy similarity1
Modified residuei417PhosphoserineBy similarity1
Modified residuei422PhosphoserineCombined sources1
Modified residuei480N6-acetyllysine; alternateBy similarity1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei499N6-acetyllysineBy similarity1
Modified residuei511PhosphothreonineCombined sources1
Modified residuei515PhosphoserineCombined sources1
Modified residuei517PhosphoserineCombined sources1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP04040.
MaxQBiP04040.
PaxDbiP04040.
PeptideAtlasiP04040.
PRIDEiP04040.

2D gel databases

OGPiP04040.
REPRODUCTION-2DPAGEIPI00465436.
P04040.
SWISS-2DPAGEP04040.

PTM databases

iPTMnetiP04040.
PhosphoSitePlusiP04040.
SwissPalmiP04040.

Expressioni

Gene expression databases

BgeeiENSG00000121691.
CleanExiHS_CAT.
GenevisibleiP04040. HS.

Organism-specific databases

HPAiCAB001515.
HPA051282.
HPA055838.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107297. 48 interactors.
IntActiP04040. 21 interactors.
MINTiMINT-1210583.
STRINGi9606.ENSP00000241052.

Structurei

Secondary structure

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 10Combined sources4
Helixi11 – 18Combined sources8
Turni19 – 21Combined sources3
Beta strandi30 – 32Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi42 – 45Combined sources4
Helixi55 – 64Combined sources10
Beta strandi73 – 75Combined sources3
Beta strandi77 – 87Combined sources11
Turni92 – 94Combined sources3
Helixi98 – 100Combined sources3
Beta strandi106 – 114Combined sources9
Beta strandi116 – 118Combined sources3
Beta strandi124 – 128Combined sources5
Beta strandi131 – 138Combined sources8
Beta strandi141 – 152Combined sources12
Helixi158 – 160Combined sources3
Helixi161 – 168Combined sources8
Turni172 – 174Combined sources3
Helixi179 – 188Combined sources10
Helixi190 – 192Combined sources3
Helixi193 – 199Combined sources7
Helixi202 – 204Combined sources3
Beta strandi205 – 209Combined sources5
Beta strandi220 – 223Combined sources4
Beta strandi229 – 238Combined sources10
Helixi247 – 256Combined sources10
Helixi260 – 270Combined sources11
Beta strandi276 – 284Combined sources9
Helixi286 – 291Combined sources6
Turni305 – 307Combined sources3
Beta strandi311 – 320Combined sources10
Helixi325 – 328Combined sources4
Turni329 – 331Combined sources3
Beta strandi343 – 345Combined sources3
Helixi349 – 365Combined sources17
Helixi370 – 372Combined sources3
Helixi374 – 376Combined sources3
Turni397 – 400Combined sources4
Beta strandi404 – 406Combined sources3
Helixi416 – 418Combined sources3
Beta strandi427 – 431Combined sources5
Helixi441 – 449Combined sources9
Helixi453 – 467Combined sources15
Helixi472 – 485Combined sources14
Helixi487 – 500Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGBX-ray2.20A/B/C/D4-501[»]
1DGFX-ray1.50A/B/C/D5-501[»]
1DGGX-ray1.80A/B/C/D5-501[»]
1DGHX-ray2.00A/B/C/D4-501[»]
1F4JX-ray2.40A/B/C/D1-527[»]
1QQWX-ray2.75A/B/C/D1-527[»]
ProteinModelPortaliP04040.
SMRiP04040.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04040.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
HOVERGENiHBG003986.
InParanoidiP04040.
KOiK03781.
OMAiWDYRADD.
OrthoDBiEOG091G04V5.
PhylomeDBiP04040.
TreeFamiTF300540.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF
110 120 130 140 150
EHIGKKTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA
260 270 280 290 300
ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT
310 320 330 340 350
KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG
410 420 430 440 450
APNYYPNSFG APEQQPSALE HSIQYSGEVR RFNTANDDNV TQVRAFYVNV
460 470 480 490 500
LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK NFTEVHPDYG SHIQALLDKY
510 520
NAEKPKNAIH TFVQSGSHLA AREKANL
Length:527
Mass (Da):59,756
Last modified:January 23, 2007 - v3
Checksum:i7BAA2394D124ED20
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54D → N in AAK29181 (PubMed:11728823).Curated1
Sequence conflicti100F → L in BAG37746 (PubMed:14702039).Curated1
Sequence conflicti239D → G in AAK29181 (PubMed:11728823).Curated1
Sequence conflicti274Y → D in AAK29181 (PubMed:11728823).Curated1
Sequence conflicti301K → R in AAK29181 (PubMed:11728823).Curated1
Sequence conflicti366L → P in BAG37746 (PubMed:14702039).Curated1
Sequence conflicti449N → D in BAG37746 (PubMed:14702039).Curated1
Sequence conflicti514Q → R in AAK29181 (PubMed:11728823).Curated1
Sequence conflicti520A → V in AAK29181 (PubMed:11728823).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04085
, X04086, X04087, X04088, X04089, X04090, X04091, X04092, X04093, X04094, X04095, X04096 Genomic DNA. Translation: CAA27721.1.
X04076 mRNA. Translation: CAA27717.1.
AY028632 mRNA. Translation: AAK29181.1.
AK291585 mRNA. Translation: BAF84274.1.
AK315350 mRNA. Translation: BAG37746.1.
AY545477 Genomic DNA. Translation: AAS37679.1.
AL035079 Genomic DNA. Translation: CAB45236.1.
CH471064 Genomic DNA. Translation: EAW68170.1.
CH471064 Genomic DNA. Translation: EAW68171.1.
BC110398 mRNA. Translation: AAI10399.1.
BC112217 mRNA. Translation: AAI12218.1.
BC112219 mRNA. Translation: AAI12220.1.
L13609 Genomic DNA. Translation: AAA16651.1.
K02400 Genomic DNA. Translation: AAB59522.1.
CCDSiCCDS7891.1.
PIRiA23646. CSHU.
RefSeqiNP_001743.1. NM_001752.3.
UniGeneiHs.502302.

Genome annotation databases

EnsembliENST00000241052; ENSP00000241052; ENSG00000121691.
GeneIDi847.
KEGGihsa:847.
UCSCiuc001mvm.4. human.

Cross-referencesi

Web resourcesi

Wikipedia

Catalase entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04085
, X04086, X04087, X04088, X04089, X04090, X04091, X04092, X04093, X04094, X04095, X04096 Genomic DNA. Translation: CAA27721.1.
X04076 mRNA. Translation: CAA27717.1.
AY028632 mRNA. Translation: AAK29181.1.
AK291585 mRNA. Translation: BAF84274.1.
AK315350 mRNA. Translation: BAG37746.1.
AY545477 Genomic DNA. Translation: AAS37679.1.
AL035079 Genomic DNA. Translation: CAB45236.1.
CH471064 Genomic DNA. Translation: EAW68170.1.
CH471064 Genomic DNA. Translation: EAW68171.1.
BC110398 mRNA. Translation: AAI10399.1.
BC112217 mRNA. Translation: AAI12218.1.
BC112219 mRNA. Translation: AAI12220.1.
L13609 Genomic DNA. Translation: AAA16651.1.
K02400 Genomic DNA. Translation: AAB59522.1.
CCDSiCCDS7891.1.
PIRiA23646. CSHU.
RefSeqiNP_001743.1. NM_001752.3.
UniGeneiHs.502302.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGBX-ray2.20A/B/C/D4-501[»]
1DGFX-ray1.50A/B/C/D5-501[»]
1DGGX-ray1.80A/B/C/D5-501[»]
1DGHX-ray2.00A/B/C/D4-501[»]
1F4JX-ray2.40A/B/C/D1-527[»]
1QQWX-ray2.75A/B/C/D1-527[»]
ProteinModelPortaliP04040.
SMRiP04040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107297. 48 interactors.
IntActiP04040. 21 interactors.
MINTiMINT-1210583.
STRINGi9606.ENSP00000241052.

Chemistry databases

ChEMBLiCHEMBL3627594.
DrugBankiDB01213. Fomepizole.

Protein family/group databases

PeroxiBasei5282. HsKat01.

PTM databases

iPTMnetiP04040.
PhosphoSitePlusiP04040.
SwissPalmiP04040.

Polymorphism and mutation databases

BioMutaiCAT.
DMDMi115702.

2D gel databases

OGPiP04040.
REPRODUCTION-2DPAGEIPI00465436.
P04040.
SWISS-2DPAGEP04040.

Proteomic databases

EPDiP04040.
MaxQBiP04040.
PaxDbiP04040.
PeptideAtlasiP04040.
PRIDEiP04040.

Protocols and materials databases

DNASUi847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241052; ENSP00000241052; ENSG00000121691.
GeneIDi847.
KEGGihsa:847.
UCSCiuc001mvm.4. human.

Organism-specific databases

CTDi847.
DisGeNETi847.
GeneCardsiCAT.
H-InvDBHIX0009550.
HGNCiHGNC:1516. CAT.
HPAiCAB001515.
HPA051282.
HPA055838.
MalaCardsiCAT.
MIMi115500. gene.
614097. phenotype.
neXtProtiNX_P04040.
OpenTargetsiENSG00000121691.
Orphaneti926. Acatalasemia.
PharmGKBiPA26099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
HOVERGENiHBG003986.
InParanoidiP04040.
KOiK03781.
OMAiWDYRADD.
OrthoDBiEOG091G04V5.
PhylomeDBiP04040.
TreeFamiTF300540.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-341.
ZFISH:MONOMER66-341.
BRENDAi1.11.1.6. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-74259. Purine catabolism.
SABIO-RKP04040.
SIGNORiP04040.

Miscellaneous databases

ChiTaRSiCAT. human.
EvolutionaryTraceiP04040.
GeneWikiiCatalase.
GenomeRNAii847.
PROiP04040.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121691.
CleanExiHS_CAT.
GenevisibleiP04040. HS.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATA_HUMAN
AccessioniPrimary (citable) accession number: P04040
Secondary accession number(s): A8K6C0
, B2RCZ9, D3DR07, Q2M1U4, Q4VXX5, Q9BWT9, Q9UC85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 194 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.