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Catalase (EC 1.11.1.6)

 CATA_HUMAN              Reviewed;         527 AA.
P04040; A8K6C0; B2RCZ9; D3DR07; Q2M1U4; Q4VXX5; Q9BWT9; Q9UC85;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 202.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=CAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3755525; DOI=10.1093/nar/14.13.5321;
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;
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;
PubMed=11728823; DOI=10.1016/S0891-5849(01)00734-1;
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;
PubMed=14702039; DOI=10.1038/ng1285;
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 variation discovery resource;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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; DOI=10.1172/JCI116959;
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;
PubMed=12665801; DOI=10.1038/nbt810;
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;
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;
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 IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[14]
INVOLVEMENT IN ACATLAS.
PubMed=2308162; DOI=10.1016/0022-2836(90)90359-T;
Wen J.K., Osumi T., Hashimoto T., Ogata M.;
"Molecular analysis of human acatalasemia. Identification of a
splicing mutation.";
J. Mol. Biol. 211:383-393(1990).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-422; THR-511;
SER-515 AND SER-517, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
PubMed=10666617; DOI=10.1107/S0907444999015930;
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).
[22]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=10656833; DOI=10.1006/jmbi.1999.3458;
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).
[23]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=11134921; DOI=10.1107/S0907444900013767;
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).
-!- 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.
{ECO:0000269|PubMed:7882369}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013,
ECO:0000269|PubMed:7882369}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- PTM: The N-terminus is blocked.
-!- 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.
{ECO:0000269|PubMed:2308162}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Catalase entry;
URL="https://en.wikipedia.org/wiki/Catalase";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cat/";
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EMBL; X04085; CAA27721.1; -; Genomic_DNA.
EMBL; X04086; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04087; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04088; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04089; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04090; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04091; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04092; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04093; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04094; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04095; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04096; CAA27721.1; JOINED; Genomic_DNA.
EMBL; X04076; CAA27717.1; -; mRNA.
EMBL; AY028632; AAK29181.1; -; mRNA.
EMBL; AK291585; BAF84274.1; -; mRNA.
EMBL; AK315350; BAG37746.1; -; mRNA.
EMBL; AY545477; AAS37679.1; -; Genomic_DNA.
EMBL; AL035079; CAB45236.1; -; Genomic_DNA.
EMBL; CH471064; EAW68170.1; -; Genomic_DNA.
EMBL; CH471064; EAW68171.1; -; Genomic_DNA.
EMBL; BC110398; AAI10399.1; -; mRNA.
EMBL; BC112217; AAI12218.1; -; mRNA.
EMBL; BC112219; AAI12220.1; -; mRNA.
EMBL; L13609; AAA16651.1; -; Genomic_DNA.
EMBL; K02400; AAB59522.1; -; Genomic_DNA.
CCDS; CCDS7891.1; -.
PIR; A23646; CSHU.
RefSeq; NP_001743.1; NM_001752.3.
UniGene; Hs.502302; -.
PDB; 1DGB; X-ray; 2.20 A; A/B/C/D=4-501.
PDB; 1DGF; X-ray; 1.50 A; A/B/C/D=5-501.
PDB; 1DGG; X-ray; 1.80 A; A/B/C/D=5-501.
PDB; 1DGH; X-ray; 2.00 A; A/B/C/D=4-501.
PDB; 1F4J; X-ray; 2.40 A; A/B/C/D=1-527.
PDB; 1QQW; X-ray; 2.75 A; A/B/C/D=1-527.
PDBsum; 1DGB; -.
PDBsum; 1DGF; -.
PDBsum; 1DGG; -.
PDBsum; 1DGH; -.
PDBsum; 1F4J; -.
PDBsum; 1QQW; -.
ProteinModelPortal; P04040; -.
SMR; P04040; -.
BioGrid; 107297; 48.
ELM; P04040; -.
IntAct; P04040; 21.
MINT; MINT-1210583; -.
STRING; 9606.ENSP00000241052; -.
BindingDB; P04040; -.
ChEMBL; CHEMBL3627594; -.
DrugBank; DB01213; Fomepizole.
PeroxiBase; 5282; HsKat01.
iPTMnet; P04040; -.
PhosphoSitePlus; P04040; -.
SwissPalm; P04040; -.
BioMuta; CAT; -.
DMDM; 115702; -.
OGP; P04040; -.
REPRODUCTION-2DPAGE; IPI00465436; -.
REPRODUCTION-2DPAGE; P04040; -.
SWISS-2DPAGE; P04040; -.
EPD; P04040; -.
MaxQB; P04040; -.
PaxDb; P04040; -.
PeptideAtlas; P04040; -.
PRIDE; P04040; -.
DNASU; 847; -.
Ensembl; ENST00000241052; ENSP00000241052; ENSG00000121691.
GeneID; 847; -.
KEGG; hsa:847; -.
UCSC; uc001mvm.4; human.
CTD; 847; -.
DisGeNET; 847; -.
EuPathDB; HostDB:ENSG00000121691.4; -.
GeneCards; CAT; -.
H-InvDB; HIX0009550; -.
HGNC; HGNC:1516; CAT.
HPA; CAB001515; -.
HPA; HPA051282; -.
HPA; HPA055838; -.
MalaCards; CAT; -.
MIM; 115500; gene.
MIM; 614097; phenotype.
neXtProt; NX_P04040; -.
OpenTargets; ENSG00000121691; -.
Orphanet; 926; Acatalasemia.
PharmGKB; PA26099; -.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
HOVERGEN; HBG003986; -.
InParanoid; P04040; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
PhylomeDB; P04040; -.
TreeFam; TF300540; -.
BioCyc; MetaCyc:MONOMER66-341; -.
BRENDA; 1.11.1.6; 2681.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P04040; -.
SIGNOR; P04040; -.
ChiTaRS; CAT; human.
EvolutionaryTrace; P04040; -.
GeneWiki; Catalase; -.
GenomeRNAi; 847; -.
PRO; PR:P04040; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000121691; -.
CleanEx; HS_CAT; -.
Genevisible; P04040; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0014854; P:response to inactivity; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
GO; GO:0010193; P:response to ozone; IEA:Ensembl.
GO; GO:0080184; P:response to phenylpropanoid; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; IMP:UniProtKB.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0009650; P:UV protection; IMP:UniProtKB.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801}.
CHAIN 2 527 Catalase.
/FTId=PRO_0000084901.
ACT_SITE 75 75
ACT_SITE 148 148
METAL 358 358 Iron (heme axial ligand).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:25944712}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 221 221 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 306 306 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 306 306 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 480 480 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CONFLICT 54 54 D -> N (in Ref. 3; AAK29181).
{ECO:0000305}.
CONFLICT 100 100 F -> L (in Ref. 4; BAG37746).
{ECO:0000305}.
CONFLICT 239 239 D -> G (in Ref. 3; AAK29181).
{ECO:0000305}.
CONFLICT 274 274 Y -> D (in Ref. 3; AAK29181).
{ECO:0000305}.
CONFLICT 301 301 K -> R (in Ref. 3; AAK29181).
{ECO:0000305}.
CONFLICT 366 366 L -> P (in Ref. 4; BAG37746).
{ECO:0000305}.
CONFLICT 449 449 N -> D (in Ref. 4; BAG37746).
{ECO:0000305}.
CONFLICT 514 514 Q -> R (in Ref. 3; AAK29181).
{ECO:0000305}.
CONFLICT 520 520 A -> V (in Ref. 3; AAK29181).
{ECO:0000305}.
TURN 7 10 {ECO:0000244|PDB:1DGF}.
HELIX 11 18 {ECO:0000244|PDB:1DGF}.
TURN 19 21 {ECO:0000244|PDB:1DGF}.
STRAND 30 32 {ECO:0000244|PDB:1QQW}.
STRAND 38 40 {ECO:0000244|PDB:1DGF}.
STRAND 42 45 {ECO:0000244|PDB:1DGF}.
HELIX 55 64 {ECO:0000244|PDB:1DGF}.
STRAND 73 75 {ECO:0000244|PDB:1F4J}.
STRAND 77 87 {ECO:0000244|PDB:1DGF}.
TURN 92 94 {ECO:0000244|PDB:1DGF}.
HELIX 98 100 {ECO:0000244|PDB:1DGF}.
STRAND 106 114 {ECO:0000244|PDB:1DGF}.
STRAND 116 118 {ECO:0000244|PDB:1DGF}.
STRAND 124 128 {ECO:0000244|PDB:1DGF}.
STRAND 131 138 {ECO:0000244|PDB:1DGF}.
STRAND 141 152 {ECO:0000244|PDB:1DGF}.
HELIX 158 160 {ECO:0000244|PDB:1DGF}.
HELIX 161 168 {ECO:0000244|PDB:1DGF}.
TURN 172 174 {ECO:0000244|PDB:1DGF}.
HELIX 179 188 {ECO:0000244|PDB:1DGF}.
HELIX 190 192 {ECO:0000244|PDB:1DGF}.
HELIX 193 199 {ECO:0000244|PDB:1DGF}.
HELIX 202 204 {ECO:0000244|PDB:1DGF}.
STRAND 205 209 {ECO:0000244|PDB:1DGF}.
STRAND 220 223 {ECO:0000244|PDB:1DGF}.
STRAND 229 238 {ECO:0000244|PDB:1DGF}.
HELIX 247 256 {ECO:0000244|PDB:1DGF}.
HELIX 260 270 {ECO:0000244|PDB:1DGF}.
STRAND 276 284 {ECO:0000244|PDB:1DGF}.
HELIX 286 291 {ECO:0000244|PDB:1DGF}.
TURN 305 307 {ECO:0000244|PDB:1DGF}.
STRAND 311 320 {ECO:0000244|PDB:1DGF}.
HELIX 325 328 {ECO:0000244|PDB:1DGF}.
TURN 329 331 {ECO:0000244|PDB:1DGF}.
STRAND 343 345 {ECO:0000244|PDB:1DGF}.
HELIX 349 365 {ECO:0000244|PDB:1DGF}.
HELIX 370 372 {ECO:0000244|PDB:1DGF}.
HELIX 374 376 {ECO:0000244|PDB:1DGF}.
TURN 397 400 {ECO:0000244|PDB:1DGF}.
STRAND 404 406 {ECO:0000244|PDB:1DGF}.
HELIX 416 418 {ECO:0000244|PDB:1DGF}.
STRAND 427 431 {ECO:0000244|PDB:1DGF}.
HELIX 441 449 {ECO:0000244|PDB:1DGF}.
HELIX 453 467 {ECO:0000244|PDB:1DGF}.
HELIX 472 485 {ECO:0000244|PDB:1DGF}.
HELIX 487 500 {ECO:0000244|PDB:1DGF}.
SEQUENCE 527 AA; 59756 MW; 7BAA2394D124ED20 CRC64;
MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ
GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT
KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD
THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE
HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK
NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL


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