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P04040

- CATA_HUMAN

UniProt

P04040 - CATA_HUMAN

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Protein

Catalase

Gene

CAT

Organism
Homo sapiens (Human)
Status
Reviewed - 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.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. menopause Source: Ensembl
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  9. nucleobase-containing small molecule metabolic process Source: Reactome
  10. osteoblast differentiation Source: UniProt
  11. positive regulation of cell division Source: UniProtKB-KW
  12. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  13. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  14. protein homotetramerization Source: UniProtKB
  15. protein tetramerization Source: UniProtKB
  16. purine nucleobase metabolic process Source: Reactome
  17. purine nucleotide catabolic process Source: Reactome
  18. response to hyperoxia Source: Ensembl
  19. response to hypoxia Source: Ensembl
  20. response to reactive oxygen species Source: UniProtKB
  21. response to vitamin E Source: Ensembl
  22. small molecule metabolic process Source: Reactome
  23. triglyceride metabolic process Source: Ensembl
  24. ureteric bud development Source: Ensembl
  25. UV protection Source: UniProtKB
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.
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: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. Golgi apparatus Source: Ensembl
  6. intracellular membrane-bounded organelle Source: HPA
  7. lysosome Source: Ensembl
  8. membrane Source: UniProtKB
  9. mitochondrial intermembrane space Source: Ensembl
  10. peroxisomal matrix Source: Reactome
  11. peroxisomal membrane Source: UniProtKB
  12. peroxisome Source: UniProtKB
  13. plasma membrane Source: Ensembl
Complete GO annotation...

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

BgeeiP04040.
CleanExiHS_CAT.
ExpressionAtlasiP04040. baseline and differential.
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.
GeneTreeiENSGT00390000018100.
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

        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)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.
GeneTreei ENSGT00390000018100.
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

Bgeei P04040.
CleanExi HS_CAT.
ExpressionAtlasi P04040. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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