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UniProtKB/Swiss-Prot entry P04040


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATA_HUMAN
Primary accession number P04040
Secondary accession numbers A8K6C0 B2RCZ9 Q2M1U4 Q4VXX5 Q9BWT9 Q9UC85
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 109)
Name and origin of the protein
Protein name Catalase
Synonym EC 1.11.1.6
Gene name
Name: CAT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/14.13.5321; PubMed=3755525 [NCBI, ExPASy, EBI, Israel, Japan]
Quan F., Korneluk R.G., Tropak M.B., Gravel R.A.;
"Isolation and characterization of the human catalase gene.";
Nucleic Acids Res. 14:5321-5335(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=3755526 [NCBI, ExPASy, EBI, Israel, Japan]
Bell G.I., Najarian R.C., Mullenbach G.T., Hallewell R.A.;
"cDNA sequence coding for human kidney catalase.";
Nucleic Acids Res. 14:5561-5562(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/S0891-5849(01)00734-1; PubMed=11728823 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells.";
Free Radic. Biol. Med. 31:1509-1519(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Uterus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04632; PubMed=16554811 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=8282800 [NCBI, ExPASy, EBI, Israel, Japan]
Yoo J.-H., Erzurum S.C., Hay J.G., Lemarchand P., Crystal R.G.;
"Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress.";
J. Clin. Invest. 93:297-302(1994).
[10]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 24-38; 99-105; 307-315 AND 469-476, FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=Erythrocyte;
PubMed=7882369 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi A., Miyamoto T., Yamaji K., Masuho Y., Hayashi M., Hayashi H., Onozaki K.;
"A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase.";
Cancer Res. 55:1586-1589(1995).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-527.
TISSUE=Fibroblast;
PubMed=6548744 [NCBI, ExPASy, EBI, Israel, Japan]
Korneluk R.G., Quan F., Lewis W.H., Guise K.S., Willard H.F., Holmes M.T., Gravel R.A.;
"Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA.";
J. Biol. Chem. 259:13819-13823(1984).
[13]
PROTEIN SEQUENCE OF 445-456, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231 AND TYR-308, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[15]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
DOI=10.1107/S0907444999015930; PubMed=10666617 [NCBI, ExPASy, EBI, Israel, Japan]
Ko T.P., Safo M.K., Musayev F.N., Di Salvo M.L., Wang C., Wu S.H., Abraham D.J.;
"Structure of human erythrocyte catalase.";
Acta Crystallogr. D 56:241-245(2000).
[16]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
DOI=10.1006/jmbi.1999.3458; PubMed=10656833 [NCBI, ExPASy, EBI, Israel, Japan]
Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A.;
"Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.";
J. Mol. Biol. 296:295-309(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1107/S0907444900013767; PubMed=11134921 [NCBI, ExPASy, EBI, Israel, Japan]
Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P.;
"Structure of tetragonal crystals of human erythrocyte catalase.";
Acta Crystallogr. D 57:1-7(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04085; CAA27721.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04086; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04087; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04088; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04089; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04090; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04091; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04092; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04093; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04094; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04095; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04096; CAA27721.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04076; CAA27717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY028632; AAK29181.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291585; BAF84274.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK315350; BAG37746.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY545477; AAS37679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035079; CAB45236.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471064; EAW68170.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110398; AAI10399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112217; AAI12218.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112219; AAI12220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13609; AAA16651.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02400; AAB59522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23646; CSHU.
RefSeq NP_001743.1; -.
UniGene Hs.502302
3D structure databases
PDB
1DGB; X-ray; 2.20 A; A/B/C/D=4-501.[ExPASy / RCSB / EBI]
1DGF; X-ray; 1.50 A; A/B/C/D=5-501.[ExPASy / RCSB / EBI]
1DGG; X-ray; 1.80 A; A/B/C/D=5-501.[ExPASy / RCSB / EBI]
1DGH; X-ray; 2.00 A; A/B/C/D=4-501.[ExPASy / RCSB / EBI]
1F4J; X-ray; 2.40 A; A/B/C/D=1-527.[ExPASy / RCSB / EBI]
1QQW; X-ray; 2.75 A; A/B/C/D=1-527.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DGB; -.
1DGF; -.
1DGG; -.
1DGH; -.
1F4J; -.
1QQW; -.
ModBase P04040.
Protein family/group databases
PeroxiBase 5282; HsKat01.
PTM databases
PhosphoSite P04040; -.
Enzyme and pathway databases
Reactome REACT_9522; Breakdown of hydrogen peroxide to water and molecular oxygen.
2D gel databases
SWISS-2DPAGE P04040; -.
Aarhus/Ghent-2DPAGE 1524; IEF.
1525; IEF.
1526; IEF.
OGP P04040; -.
REPRODUCTION-2DPAGE IPI00465436; -.
P04040; -.
Organism-specific databases
H-InvDB HIX0009550; -.
HIX0058959; -.
HGNC HGNC:1516; CAT.
GenAtlas CAT.
HPA CAB001515; -.
MIM 115500; gene+phenotype. [NCBI / EBI]
Orphanet 926; Acatalasemia.
PharmGKB PA26099; -.
GeneCards P04040.
Gene expression databases
ArrayExpress P04040; -.
CleanEx HS_CAT; -.
GermOnline ENSG00000121691; Homo sapiens.
Ontologies
GO
GO:0005778; Cellular component: peroxisomal membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0004096; Molecular function: catalase activity (inferred from direct assay from UniProtKB).
GO:0020037; Molecular function: heme binding (inferred from direct assay from UniProtKB).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050661; Molecular function: NADP binding (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from direct assay from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0051262; Biological process: protein tetramerization (inferred from direct assay from UniProtKB).
GO:0009650; Biological process: UV protection (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
Pfam graphical view of domain structure.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P04040.
Proteomic databases
PeptideAtlas P04040; -.
Genome annotation databases
Ensembl ENSG00000121691; Homo sapiens. [Contig view]
GeneID 847; -.
KEGG hsa:847; -.
NMPDR fig|9606.3.peg.5453; -.
Phylogenomic databases
HOGENOM P04040; -.
HOVERGEN P04040; -.
Other
DrugBank DB01213; Fomepizole.
NextBio 3550; -.
SOURCE CAT; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   527  526     Catalase. PRO_0000084901
ACT_SITE   75    75         
ACT_SITE   148   148         
METAL   358   358        Iron (heme axial ligand). 
MOD_RES   231   231        Phosphotyrosine. 
MOD_RES   308   308        Phosphotyrosine. 
MOD_RES   422   422        Phosphoserine (By similarity). 
MOD_RES   517   517        Phosphoserine (By similarity). 
CONFLICT   54    54        D -> N (in Ref. 3; AAK29181). 
CONFLICT   100   100        F -> L (in Ref. 4; BAG37746). 
CONFLICT   239   239        D -> G (in Ref. 3; AAK29181). 
CONFLICT   274   274        Y -> D (in Ref. 3; AAK29181). 
CONFLICT   301   301        K -> R (in Ref. 3; AAK29181). 
CONFLICT   366   366        L -> P (in Ref. 4; BAG37746). 
CONFLICT   449   449        N -> D (in Ref. 4; BAG37746). 
CONFLICT   514   514        Q -> R (in Ref. 3; AAK29181). 
CONFLICT   520   520        A -> V (in Ref. 3; AAK29181). 
HELIX   7    10  4      
HELIX   11    17  7      
TURN   18    21  4      
STRAND   38    40  3      
STRAND   42    45  4      
HELIX   55    64  10      
STRAND   77    87  11      
TURN   92    94  3      
HELIX   98   100  3      
STRAND   106   114  9      
STRAND   116   118  3      
STRAND   124   128  5      
STRAND   131   138  8      
STRAND   141   151  11      
HELIX   158   160  3      
HELIX   161   168  8      
TURN   172   174  3      
HELIX   179   188  10      
HELIX   190   192  3      
HELIX   193   199  7      
HELIX   202   204  3      
STRAND   205   209  5      
STRAND   220   223  4      
STRAND   229   238  10      
HELIX   247   256  10      
HELIX   260   270  11      
STRAND   276   284  9      
HELIX   286   291  6      
TURN   305   307  3      
STRAND   311   320  10      
HELIX   325   328  4      
STRAND   343   345  3      
HELIX   349   365  17      
HELIX   370   372  3      
HELIX   374   376  3      
TURN   397   400  4      
STRAND   404   406  3      
HELIX