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Protein

Catalase

Gene

CAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

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

GO - Molecular functioni

  • aminoacylase activity Source: Ensembl
  • antioxidant activity Source: UniProtKB
  • catalase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: UniProtKB
  • oxidoreductase activity, acting on peroxide as acceptor Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

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.
BRENDAi1.11.1.6. 2681.
ReactomeiREACT_2086. Purine catabolism.
REACT_264249. Detoxification of Reactive Oxygen Species.
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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1516. CAT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • lysosome Source: Ensembl
  • membrane Source: UniProtKB
  • mitochondrial intermembrane space Source: Ensembl
  • peroxisomal matrix Source: Reactome
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Acatalasemia (ACATLAS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disorder characterized by a total or near total loss of catalase activity in red cells. It is often associated with ulcerating oral lesions.

See also OMIM:614097

Organism-specific databases

MIMi614097. phenotype.
Orphaneti926. Acatalasemia.
PharmGKBiPA26099.

Chemistry

DrugBankiDB01213. Fomepizole.

Polymorphism and mutation databases

BioMutaiCAT.
DMDMi115702.

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 residuei9 – 91Phosphoserine1 Publication
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 residuei422 – 4221Phosphoserine1 Publication
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei511 – 5111Phosphothreonine1 Publication
Modified residuei515 – 5151Phosphoserine1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication

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.
GenevestigatoriP04040.

Organism-specific databases

HPAiCAB001515.
HPA051282.
HPA055838.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi107297. 16 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 – 104Combined sources
Helixi11 – 188Combined sources
Turni19 – 213Combined sources
Beta strandi30 – 323Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 454Combined sources
Helixi55 – 6410Combined sources
Beta strandi73 – 753Combined sources
Beta strandi77 – 8711Combined sources
Turni92 – 943Combined sources
Helixi98 – 1003Combined sources
Beta strandi106 – 1149Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi141 – 15212Combined sources
Helixi158 – 1603Combined sources
Helixi161 – 1688Combined sources
Turni172 – 1743Combined sources
Helixi179 – 18810Combined sources
Helixi190 – 1923Combined sources
Helixi193 – 1997Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi229 – 23810Combined sources
Helixi247 – 25610Combined sources
Helixi260 – 27011Combined sources
Beta strandi276 – 2849Combined sources
Helixi286 – 2916Combined sources
Turni305 – 3073Combined sources
Beta strandi311 – 32010Combined sources
Helixi325 – 3284Combined sources
Turni329 – 3313Combined sources
Beta strandi343 – 3453Combined sources
Helixi349 – 36517Combined sources
Helixi370 – 3723Combined sources
Helixi374 – 3763Combined sources
Turni397 – 4004Combined sources
Beta strandi404 – 4063Combined sources
Helixi416 – 4183Combined sources
Beta strandi427 – 4315Combined sources
Helixi441 – 4499Combined sources
Helixi453 – 46715Combined sources
Helixi472 – 48514Combined sources
Helixi487 – 50014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiRNPRNFF.
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:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Web resourcesi

Wikipedia

Catalase entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107297. 16 interactions.
IntActiP04040. 15 interactions.
MINTiMINT-1210583.
STRINGi9606.ENSP00000241052.

Chemistry

DrugBankiDB01213. Fomepizole.

Protein family/group databases

PeroxiBasei5282. HsKat01.

PTM databases

PhosphoSiteiP04040.

Polymorphism and mutation databases

BioMutaiCAT.
DMDMi115702.

2D gel databases

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

Proteomic databases

MaxQBiP04040.
PaxDbiP04040.
PeptideAtlasiP04040.
PRIDEiP04040.

Protocols and materials databases

DNASUi847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241052; ENSP00000241052; ENSG00000121691.
GeneIDi847.
KEGGihsa:847.
UCSCiuc001mvm.3. human.

Organism-specific databases

CTDi847.
GeneCardsiGC11P034460.
H-InvDBHIX0009550.
HGNCiHGNC:1516. CAT.
HPAiCAB001515.
HPA051282.
HPA055838.
MIMi115500. gene.
614097. phenotype.
neXtProtiNX_P04040.
Orphaneti926. Acatalasemia.
PharmGKBiPA26099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOVERGENiHBG003986.
InParanoidiP04040.
KOiK03781.
OMAiRNPRNFF.
OrthoDBiEOG7V7660.
PhylomeDBiP04040.
TreeFamiTF300540.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-341.
BRENDAi1.11.1.6. 2681.
ReactomeiREACT_2086. Purine catabolism.
REACT_264249. Detoxification of Reactive Oxygen Species.
SABIO-RKP04040.

Miscellaneous databases

ChiTaRSiCAT. human.
EvolutionaryTraceiP04040.
GeneWikiiCatalase.
GenomeRNAii847.
NextBioi3550.
PROiP04040.
SOURCEiSearch...

Gene expression databases

BgeeiP04040.
CleanExiHS_CAT.
GenevestigatoriP04040.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-422; THR-511; SER-515 AND SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
  20. "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).
  21. "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: May 27, 2015
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.