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P04040

- CATA_HUMAN

UniProt

P04040 - CATA_HUMAN

Protein

Catalase

Gene

CAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Heme group.
    NADP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei75 – 751
    Active sitei148 – 1481
    Metal bindingi358 – 3581Iron (heme axial ligand)

    GO - Molecular functioni

    1. aminoacylase activity Source: Ensembl
    2. antioxidant activity Source: UniProtKB
    3. catalase activity Source: UniProtKB
    4. enzyme binding Source: UniProtKB
    5. heme binding Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. NADP binding Source: UniProtKB
    8. oxidoreductase activity, acting on peroxide as acceptor Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB
    10. receptor binding Source: UniProtKB

    GO - Biological processi

    1. aerobic respiration Source: Ensembl
    2. cellular response to growth factor stimulus Source: Ensembl
    3. cholesterol metabolic process Source: Ensembl
    4. hemoglobin metabolic process Source: Ensembl
    5. hydrogen peroxide catabolic process Source: UniProtKB
    6. kidney development Source: Ensembl
    7. menopause Source: Ensembl
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    10. nucleobase-containing small molecule metabolic process Source: Reactome
    11. osteoblast differentiation Source: UniProt
    12. positive regulation of cell division Source: UniProtKB-KW
    13. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    14. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    15. protein homotetramerization Source: UniProtKB
    16. protein tetramerization Source: UniProtKB
    17. purine nucleobase metabolic process Source: Reactome
    18. purine nucleotide catabolic process Source: Reactome
    19. response to hyperoxia Source: Ensembl
    20. response to hypoxia Source: Ensembl
    21. response to reactive oxygen species Source: UniProtKB
    22. response to vitamin E Source: Ensembl
    23. small molecule metabolic process Source: Reactome
    24. triglyceride metabolic process Source: Ensembl
    25. ureteric bud development Source: Ensembl
    26. UV protection Source: UniProtKB

    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.
    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_2086. Purine catabolism.
    SABIO-RKP04040.

    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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1516. CAT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: Ensembl
    5. intracellular membrane-bounded organelle Source: HPA
    6. lysosome Source: Ensembl
    7. membrane Source: UniProtKB
    8. mitochondrial intermembrane space Source: Ensembl
    9. peroxisomal matrix Source: Reactome
    10. peroxisomal membrane Source: UniProtKB
    11. peroxisome Source: UniProtKB
    12. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614097. phenotype.
    Orphaneti926. Acatalasemia.
    PharmGKBiPA26099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 527526CatalasePRO_0000084901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei221 – 2211N6-succinyllysineBy similarity
    Modified residuei233 – 2331N6-acetyllysineBy similarity
    Modified residuei306 – 3061N6-acetyllysine; alternateBy similarity
    Modified residuei306 – 3061N6-succinyllysine; alternateBy similarity
    Modified residuei417 – 4171PhosphoserineBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei499 – 4991N6-acetyllysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04040.
    PaxDbiP04040.
    PeptideAtlasiP04040.
    PRIDEiP04040.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP04040.

    Expressioni

    Gene expression databases

    ArrayExpressiP04040.
    BgeeiP04040.
    CleanExiHS_CAT.
    GenevestigatoriP04040.

    Organism-specific databases

    HPAiCAB001515.
    HPA055838.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi107297. 13 interactions.
    IntActiP04040. 15 interactions.
    MINTiMINT-1210583.
    STRINGi9606.ENSP00000241052.

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104
    Helixi11 – 188
    Turni19 – 213
    Beta strandi30 – 323
    Beta strandi38 – 403
    Beta strandi42 – 454
    Helixi55 – 6410
    Beta strandi73 – 753
    Beta strandi77 – 8711
    Turni92 – 943
    Helixi98 – 1003
    Beta strandi106 – 1149
    Beta strandi116 – 1183
    Beta strandi124 – 1285
    Beta strandi131 – 1388
    Beta strandi141 – 15212
    Helixi158 – 1603
    Helixi161 – 1688
    Turni172 – 1743
    Helixi179 – 18810
    Helixi190 – 1923
    Helixi193 – 1997
    Helixi202 – 2043
    Beta strandi205 – 2095
    Beta strandi220 – 2234
    Beta strandi229 – 23810
    Helixi247 – 25610
    Helixi260 – 27011
    Beta strandi276 – 2849
    Helixi286 – 2916
    Turni305 – 3073
    Beta strandi311 – 32010
    Helixi325 – 3284
    Turni329 – 3313
    Beta strandi343 – 3453
    Helixi349 – 36517
    Helixi370 – 3723
    Helixi374 – 3763
    Turni397 – 4004
    Beta strandi404 – 4063
    Helixi416 – 4183
    Beta strandi427 – 4315
    Helixi441 – 4499
    Helixi453 – 46715
    Helixi472 – 48514
    Helixi487 – 50014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 5-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04040.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Phylogenomic databases

    eggNOGiCOG0753.
    HOVERGENiHBG003986.
    InParanoidiP04040.
    KOiK03781.
    OMAiEATTMIM.
    OrthoDBiEOG7V7660.
    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

    MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL    50
    LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF 100
    EHIGKKTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT 150
    PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF 200
    SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA 250
    ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT 300
    KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM 350
    LQGRLFAYPD THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG 400
    APNYYPNSFG APEQQPSALE HSIQYSGEVR RFNTANDDNV TQVRAFYVNV 450
    LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK NFTEVHPDYG SHIQALLDKY 500
    NAEKPKNAIH TFVQSGSHLA AREKANL 527
    Length:527
    Mass (Da):59,756
    Last modified:January 23, 2007 - v3
    Checksum:i7BAA2394D124ED20
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541D → N in AAK29181. (PubMed:11728823)Curated
    Sequence conflicti100 – 1001F → L in BAG37746. (PubMed:14702039)Curated
    Sequence conflicti239 – 2391D → G in AAK29181. (PubMed:11728823)Curated
    Sequence conflicti274 – 2741Y → D in AAK29181. (PubMed:11728823)Curated
    Sequence conflicti301 – 3011K → R in AAK29181. (PubMed:11728823)Curated
    Sequence conflicti366 – 3661L → P in BAG37746. (PubMed:14702039)Curated
    Sequence conflicti449 – 4491N → D in BAG37746. (PubMed:14702039)Curated
    Sequence conflicti514 – 5141Q → R in AAK29181. (PubMed:11728823)Curated
    Sequence conflicti520 – 5201A → V in AAK29181. (PubMed:11728823)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi115702.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Catalase entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7891.1.
    PIRi A23646. CSHU.
    RefSeqi NP_001743.1. NM_001752.3.
    UniGenei Hs.502302.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DGB X-ray 2.20 A/B/C/D 4-501 [» ]
    1DGF X-ray 1.50 A/B/C/D 5-501 [» ]
    1DGG X-ray 1.80 A/B/C/D 5-501 [» ]
    1DGH X-ray 2.00 A/B/C/D 4-501 [» ]
    1F4J X-ray 2.40 A/B/C/D 1-527 [» ]
    1QQW X-ray 2.75 A/B/C/D 1-527 [» ]
    ProteinModelPortali P04040.
    SMRi P04040. Positions 5-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107297. 13 interactions.
    IntActi P04040. 15 interactions.
    MINTi MINT-1210583.
    STRINGi 9606.ENSP00000241052.

    Chemistry

    DrugBanki DB01213. Fomepizole.

    Protein family/group databases

    PeroxiBasei 5282. HsKat01.

    PTM databases

    PhosphoSitei P04040.

    Polymorphism databases

    DMDMi 115702.

    2D gel databases

    OGPi P04040.
    REPRODUCTION-2DPAGE IPI00465436.
    P04040.
    SWISS-2DPAGE P04040.

    Proteomic databases

    MaxQBi P04040.
    PaxDbi P04040.
    PeptideAtlasi P04040.
    PRIDEi P04040.

    Protocols and materials databases

    DNASUi 847.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000241052 ; ENSP00000241052 ; ENSG00000121691 .
    GeneIDi 847.
    KEGGi hsa:847.
    UCSCi uc001mvm.3. human.

    Organism-specific databases

    CTDi 847.
    GeneCardsi GC11P034460.
    H-InvDB HIX0009550.
    HGNCi HGNC:1516. CAT.
    HPAi CAB001515.
    HPA055838.
    MIMi 115500. gene.
    614097. phenotype.
    neXtProti NX_P04040.
    Orphaneti 926. Acatalasemia.
    PharmGKBi PA26099.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0753.
    HOVERGENi HBG003986.
    InParanoidi P04040.
    KOi K03781.
    OMAi EATTMIM.
    OrthoDBi EOG7V7660.
    PhylomeDBi P04040.
    TreeFami TF300540.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER66-341.
    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_2086. Purine catabolism.
    SABIO-RK P04040.

    Miscellaneous databases

    ChiTaRSi CAT. human.
    EvolutionaryTracei P04040.
    GeneWikii Catalase.
    GenomeRNAii 847.
    NextBioi 3550.
    PROi P04040.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04040.
    Bgeei P04040.
    CleanExi HS_CAT.
    Genevestigatori P04040.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    InterProi IPR018028. 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 ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. 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).

    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: October 1, 2014
    This is version 170 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

    External Data

    Dasty 3