P04040 (CATA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:

CAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.11
Catalytic activity	2 H2O2 = O2 + 2 H2O. Ref.11
Cofactor	Heme group. NADP.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Post-translational modification	The N-terminus is blocked.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding NADP
Molecular function	Mitogen Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from mutant phenotype PubMed 16644728PubMed 17053817. Source: UniProtKB aerobic respiration Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cholesterol metabolic process Inferred from electronic annotation. Source: Compara hemoglobin metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from direct assay PubMed 18379038. Source: UniProtKB menopause Inferred from electronic annotation. Source: Compara negative regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16644728. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from direct assay PubMed 21976670. Source: UniProtKB purine nucleobase metabolic process Traceable author statement. Source: Reactome purine nucleotide catabolic process Traceable author statement. Source: Reactome response to hyperoxia Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to vitamin E Inferred from electronic annotation. Source: Compara triglyceride metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Inferred from electronic annotation. Source: Compara peroxisomal matrix Traceable author statement. Source: Reactome peroxisomal membrane Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	NADP binding Inferred from direct assay Ref.19. Source: UniProtKB aminoacylase activity Inferred from electronic annotation. Source: Compara catalase activity Inferred from direct assay PubMed 16644728PubMed 18312938PubMed 18379038. Source: UniProtKB heme binding Inferred from direct assay Ref.19Ref.20. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay Ref.19. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 527

526

Catalase

PRO_0000084901

Sites

Active site

75

1

Active site

148

1

Metal binding

358

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

422

1

Phosphoserine By similarity

Modified residue

517

1

Phosphoserine By similarity

Experimental info

Sequence conflict

54

1

D → N in AAK29181. Ref.3

Sequence conflict

100

1

F → L in BAG37746. Ref.4

Sequence conflict

239

1

D → G in AAK29181. Ref.3

Sequence conflict

274

1

Y → D in AAK29181. Ref.3

Sequence conflict

301

1

K → R in AAK29181. Ref.3

Sequence conflict

366

1

L → P in BAG37746. Ref.4

Sequence conflict

449

1

N → D in BAG37746. Ref.4

Sequence conflict

514

1

Q → R in AAK29181. Ref.3

Sequence conflict

520

1

A → V in AAK29181. Ref.3

Secondary structure

1

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527

Helix Strand Turn

Details...

Turn

7 – 10

4

Helix

11 – 18

8

Turn

19 – 21

3

Beta strand

30 – 32

3

Beta strand

38 – 40

3

Beta strand

42 – 45

4

Helix

55 – 64

10

Beta strand

73 – 75

3

Beta strand

77 – 87

11

Turn

92 – 94

3

Helix

98 – 100

3

Beta strand

106 – 114

9

Beta strand

116 – 118

3

Beta strand

124 – 128

5

Beta strand

131 – 138

8

Beta strand

141 – 152

12

Helix

158 – 160

3

Helix

161 – 168

8

Turn

172 – 174

3

Helix

179 – 188

10

Helix

190 – 192

3

Helix

193 – 199

7

Helix

202 – 204

3

Beta strand

205 – 209

5

Beta strand

220 – 223

4

Beta strand

229 – 238

10

Helix

247 – 256

10

Helix

260 – 270

11

Beta strand

276 – 284

9

Helix

286 – 291

6

Turn

305 – 307

3

Beta strand

311 – 320

10

Helix

325 – 328

4

Turn

329 – 331

3

Beta strand

343 – 345

3

Helix

349 – 365

17

Helix

370 – 372

3

Helix

374 – 376

3

Turn

397 – 400

4

Beta strand

404 – 406

3

Helix

416 – 418

3

Beta strand

423 – 425

3

Beta strand

427 – 431

5

Helix

441 – 449

9

Helix

453 – 467

15

Helix

472 – 485

14

Helix

487 – 500

14

Sequences

	Sequence		Length	Mass (Da)
	P04040 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7BAA2394D124ED20	FASTA	527	59,756
	10 20 30 40 50 60 MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE 70 80 90 100 110 120 MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES 130 140 150 160 170 180 GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD 190 200 210 220 230 240 MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 250 260 270 280 290 300 GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT 310 320 330 340 350 360 KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD 370 380 390 400 410 420 THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE 430 440 450 460 470 480 HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK 490 500 510 520 NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." 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. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 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, 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]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Structure of human erythrocyte catalase." Ko T.P., Safo M.K., Musayev F.N., Di Salvo M.L., Wang C., Wu S.H., Abraham D.J. Acta Crystallogr. D 56:241-245(2000) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Web resources

Wikipedia

Catalase entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00465436.

PIR

CSHU. A23646.

RefSeq

NP_001743.1. NM_001752.3.

UniGene

Hs.502302.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04040.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04040. 10 interactions.

MINT

MINT-1210583.

STRING

9606.ENSP00000241052.

Protein family/group databases

PeroxiBase

5282. HsKat01.

PTM databases

PhosphoSite

P04040.

Polymorphism databases

DMDM

115702.

2D gel databases

OGP

P04040.

REPRODUCTION-2DPAGE

IPI00465436.
P04040.

SWISS-2DPAGE

P04040.

Proteomic databases

PaxDb

P04040.

PeptideAtlas

P04040.

PRIDE

P04040.

Protocols and materials databases

DNASU

847.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000241052; ENSP00000241052; ENSG00000121691.

GeneID

847.

KEGG

hsa:847.

UCSC

uc001mvm.3. human.

Organism-specific databases

CTD

847.

GeneCards

GC11P034460.

H-InvDB

HIX0009550.

HGNC

HGNC:1516. CAT.

HPA

CAB001515.

MIM

115500. gene.
614097. phenotype.

neXtProt

NX_P04040.

Orphanet

926. Acatalasemia.

PharmGKB

PA26099.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0753.

HOVERGEN

HBG003986.

InParanoid

P04040.

KO

K03781.

OMA

HDITRYS.

OrthoDB

EOG45TCMV.

PhylomeDB

P04040.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER66-341.

Pathway_Interaction_DB

foxopathway. FoxO family signaling.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P04040.

Gene expression databases

ArrayExpress

P04040.

Bgee

P04040.

CleanEx

HS_CAT.

Genevestigator

P04040.

GermOnline

ENSG00000121691. Homo sapiens.

Family and domain databases

Gene3D

2.40.180.10. 1 hit.

InterPro

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]

PANTHER

PTHR11465. PTHR11465. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]

PIRSF

PIRSF038928. Catalase_clade1-3. 1 hit.

PRINTS

PR00067. CATALASE.

SMART

SM01060. Catalase. 1 hit.
[Graphical view]

SUPFAM

SSF56634. Catalase_N. 1 hit.

PROSITE

PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CAT. human.

DrugBank

DB01213. Fomepizole.

EvolutionaryTrace

P04040.

GenomeRNAi

847.

NextBio

3550.

SOURCE

Search...

Entry information

Entry name

CATA_HUMAN

Accession

Primary (citable) accession number: P04040
Secondary accession number(s): A8K6C0 , B2RCZ9, D3DR07, Q2M1U4, Q4VXX5, Q9BWT9, Q9UC85

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.