CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002077
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Catalase 
Protein Synonyms/Alias
  
Gene Name
 CAT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16SDQMQHWKEQRAAQKacetylation[1]
23KEQRAAQKADVLTTGubiquitination[2, 3]
38AGNPVGDKLNVITVGacetylation[1]
38AGNPVGDKLNVITVGubiquitination[3]
77PERVVHAKGAGAFGYubiquitination[3]
98ITKYSKAKVFEHIGKubiquitination[4, 5]
237VYCKFHYKTDQGIKNubiquitination[3]
243YKTDQGIKNLSVEDAacetylation[1]
243YKTDQGIKNLSVEDAubiquitination[2, 3, 4, 5]
468ENIAGHLKDAQIFIQacetylation[6]
468ENIAGHLKDAQIFIQubiquitination[3]
476DAQIFIQKKAVKNFTacetylation[1, 7, 8]
476DAQIFIQKKAVKNFTubiquitination[3]
477AQIFIQKKAVKNFTEubiquitination[3]
480FIQKKAVKNFTEVHPubiquitination[4, 5]
506KYNAEKPKNAIHTFVubiquitination[3]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 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. 
Sequence Annotation
 ACT_SITE 75 75
 ACT_SITE 148 148
 METAL 358 358 Iron (heme axial ligand).
 MOD_RES 422 422 Phosphoserine (By similarity).
 MOD_RES 517 517 Phosphoserine (By similarity).  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 527 AA 
Protein Sequence
MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE 60
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES 120
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD 180
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 240
GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT 300
KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD 360
THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE 420
HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK 480
NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL 527 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0005764; C:lysosome; IEA:Compara.
 GO:0005758; C:mitochondrial intermembrane space; IEA:Compara.
 GO:0005782; C:peroxisomal matrix; TAS:Reactome.
 GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004046; F:aminoacylase activity; IEA:Compara.
 GO:0004096; F:catalase activity; IDA:UniProtKB.
 GO:0020037; F:heme binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050661; F:NADP binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0009060; P:aerobic respiration; IEA:Compara.
 GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
 GO:0008203; P:cholesterol metabolic process; IEA:Compara.
 GO:0020027; P:hemoglobin metabolic process; IEA:Compara.
 GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
 GO:0042697; P:menopause; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Compara.
 GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Compara.
 GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
 GO:0055093; P:response to hyperoxia; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0033197; P:response to vitamin E; IEA:Compara.
 GO:0006641; P:triglyceride metabolic process; IEA:Compara.
 GO:0009650; P:UV protection; IMP:UniProtKB. 
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. 
Pfam
 PF00199; Catalase
 PF06628; Catalase-rel 
SMART
 SM01060; Catalase 
PROSITE
 PS00437; CATALASE_1
 PS00438; CATALASE_2
 PS51402; CATALASE_3 
PRINTS
 PR00067; CATALASE.