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P04040 (CATA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase

EC=1.11.1.6
Gene names
Name:CAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Catalytic activity

2 H2O2 = O2 + 2 H2O. Ref.11

Cofactor

Heme group.

NADP.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Post-translational modification

The N-terminus is blocked.

Involvement in disease

Acatalasemia (ACATLAS) [MIM:614097]: A metabolic disorder characterized by a total or near total loss of catalase activity in red cells. It is often associated with ulcerating oral lesions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processUV protection

Inferred from mutant phenotype PubMed 16644728PubMed 17053817. Source: UniProtKB

aerobic respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

hemoglobin metabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 18379038. Source: UniProtKB

kidney development

Inferred from electronic annotation. Source: Ensembl

menopause

Inferred from electronic annotation. Source: Ensembl

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16644728. Source: UniProtKB

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from direct assay PubMed 21976670. Source: UniProtKB

protein tetramerization

Inferred from direct assay Ref.19Ref.20. Source: UniProtKB

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine nucleotide catabolic process

Traceable author statement. Source: Reactome

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to reactive oxygen species

Inferred from mutant phenotype PubMed 16644728. Source: UniProtKB

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosome

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

mitochondrial intermembrane space

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 18379038PubMed 19479899PubMed 2895531PubMed 9053548. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNADP binding

Inferred from direct assay Ref.19. Source: UniProtKB

aminoacylase activity

Inferred from electronic annotation. Source: Ensembl

antioxidant activity

Inferred from direct assay PubMed 10514471. Source: UniProtKB

catalase activity

Inferred from direct assay PubMed 16644728PubMed 18312938PubMed 18379038. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16781659. Source: UniProtKB

heme binding

Inferred from direct assay Ref.19Ref.20. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on peroxide as acceptor

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.19. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365PubMed 21976670. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 527526Catalase
PRO_0000084901

Sites

Active site751
Active site1481
Metal binding3581Iron (heme axial ligand)

Amino acid modifications

Modified residue2211N6-succinyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue3061N6-acetyllysine; alternate By similarity
Modified residue3061N6-succinyllysine; alternate By similarity
Modified residue4171Phosphoserine By similarity
Modified residue4801N6-acetyllysine; alternate By similarity
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue4991N6-acetyllysine By similarity

Experimental info

Sequence conflict541D → N in AAK29181. Ref.3
Sequence conflict1001F → L in BAG37746. Ref.4
Sequence conflict2391D → G in AAK29181. Ref.3
Sequence conflict2741Y → D in AAK29181. Ref.3
Sequence conflict3011K → R in AAK29181. Ref.3
Sequence conflict3661L → P in BAG37746. Ref.4
Sequence conflict4491N → D in BAG37746. Ref.4
Sequence conflict5141Q → R in AAK29181. Ref.3
Sequence conflict5201A → V in AAK29181. Ref.3

Secondary structure

....................................................................................... 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04040 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7BAA2394D124ED20

FASTA52759,756
        10         20         30         40         50         60 
MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE 

        70         80         90        100        110        120 
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES 

       130        140        150        160        170        180 
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD 

       190        200        210        220        230        240 
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 

       250        260        270        280        290        300 
GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD 

       370        380        390        400        410        420 
THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE 

       430        440        450        460        470        480 
HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK 

       490        500        510        520 
NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the human catalase gene."
Quan F., Korneluk R.G., Tropak M.B., Gravel R.A.
Nucleic Acids Res. 14:5321-5335(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"cDNA sequence coding for human kidney catalase."
Bell G.I., Najarian R.C., Mullenbach G.T., Hallewell R.A.
Nucleic Acids Res. 14:5561-5562(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells."
Jin L.H., Bahn J.H., Eum W.S., Kwon H.Y., Jang S.H., Han K.H., Kang T.-C., Won M.H., Kang J.H., Cho S.-W., Park J., Choi S.Y.
Free Radic. Biol. Med. 31:1509-1519(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Uterus.
[5]SeattleSNPs variation discovery resource
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[9]"Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress."
Yoo J.-H., Erzurum S.C., Hay J.G., Lemarchand P., Crystal R.G.
J. Clin. Invest. 93:297-302(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[10]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Tissue: Platelet.
[11]"A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase."
Takeuchi A., Miyamoto T., Yamaji K., Masuho Y., Hayashi M., Hayashi H., Onozaki K.
Cancer Res. 55:1586-1589(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-38; 99-105; 307-315 AND 469-476, FUNCTION, CATALYTIC ACTIVITY.
Tissue: Erythrocyte.
[12]"Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA."
Korneluk R.G., Quan F., Lewis W.H., Guise K.S., Willard H.F., Holmes M.T., Gravel R.A.
J. Biol. Chem. 259:13819-13823(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-527.
Tissue: Fibroblast.
[13]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 445-456, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[14]"Molecular analysis of human acatalasemia. Identification of a splicing mutation."
Wen J.K., Osumi T., Hashimoto T., Ogata M.
J. Mol. Biol. 211:383-393(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACATLAS.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structure of human erythrocyte catalase."
Ko T.P., Safo M.K., Musayev F.N., Di Salvo M.L., Wang C., Wu S.H., Abraham D.J.
Acta Crystallogr. D 56:241-245(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[19]"Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism."
Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A.
J. Mol. Biol. 296:295-309(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[20]"Structure of tetragonal crystals of human erythrocyte catalase."
Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P.
Acta Crystallogr. D 57:1-7(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04085 expand/collapse EMBL AC list , 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.
CCDSCCDS7891.1.
PIRCSHU. A23646.
RefSeqNP_001743.1. NM_001752.3.
UniGeneHs.502302.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP04040.
SMRP04040. Positions 5-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107297. 13 interactions.
IntActP04040. 15 interactions.
MINTMINT-1210583.
STRING9606.ENSP00000241052.

Chemistry

DrugBankDB01213. Fomepizole.

Protein family/group databases

PeroxiBase5282. HsKat01.

PTM databases

PhosphoSiteP04040.

Polymorphism databases

DMDM115702.

2D gel databases

OGPP04040.
REPRODUCTION-2DPAGEIPI00465436.
P04040.
SWISS-2DPAGEP04040.

Proteomic databases

MaxQBP04040.
PaxDbP04040.
PeptideAtlasP04040.
PRIDEP04040.

Protocols and materials databases

DNASU847.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241052; ENSP00000241052; ENSG00000121691.
GeneID847.
KEGGhsa:847.
UCSCuc001mvm.3. human.

Organism-specific databases

CTD847.
GeneCardsGC11P034460.
H-InvDBHIX0009550.
HGNCHGNC:1516. CAT.
HPACAB001515.
HPA055838.
MIM115500. gene.
614097. phenotype.
neXtProtNX_P04040.
Orphanet926. Acatalasemia.
PharmGKBPA26099.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0753.
HOVERGENHBG003986.
InParanoidP04040.
KOK03781.
OMAEATTMIM.
OrthoDBEOG7V7660.
PhylomeDBP04040.
TreeFamTF300540.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER66-341.
ReactomeREACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.
SABIO-RKP04040.

Gene expression databases

ArrayExpressP04040.
BgeeP04040.
CleanExHS_CAT.
GenevestigatorP04040.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. 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]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAT. human.
EvolutionaryTraceP04040.
GeneWikiCatalase.
GenomeRNAi847.
NextBio3550.
PROP04040.
SOURCESearch...

Entry information

Entry nameCATA_HUMAN
AccessionPrimary (citable) accession number: P04040
Secondary accession number(s): A8K6C0 expand/collapse secondary AC list , B2RCZ9, D3DR07, Q2M1U4, Q4VXX5, Q9BWT9, Q9UC85
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM