CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Catalase 
Protein Synonyms/Alias
  
Gene Name
 Cat 
Gene Synonyms/Alias
 Cas-1; Cas1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
13DPASDQMKQWKEQRAubiquitination[1]
16SDQMKQWKEQRASQRacetylation[2]
38GGNPIGDKLNIMTAGacetylation[2]
38GGNPIGDKLNIMTAGubiquitination[1]
98ITRYSKAKVFEHIGKacetylation[2, 3]
98ITRYSKAKVFEHIGKsuccinylation[3]
98ITRYSKAKVFEHIGKubiquitination[1]
105KVFEHIGKRTPIAVRacetylation[2, 4]
105KVFEHIGKRTPIAVRubiquitination[1]
169PSFIHSQKRNPQTHLacetylation[4, 5]
169PSFIHSQKRNPQTHLubiquitination[1]
221GYGSHTFKLVNADGEacetylation[3, 4]
221GYGSHTFKLVNADGEsuccinylation[3]
221GYGSHTFKLVNADGEubiquitination[1]
233DGEAVYCKFHYKTDQacetylation[2, 4, 5]
237VYCKFHYKTDQGIKNacetylation[2, 4, 5]
237VYCKFHYKTDQGIKNubiquitination[1]
243YKTDQGIKNLPVGEAacetylation[5]
243YKTDQGIKNLPVGEAubiquitination[1]
301FNPFDLTKVWPHKDYubiquitination[1]
306LTKVWPHKDYPLIPVacetylation[2, 3, 4, 5]
306LTKVWPHKDYPLIPVsuccinylation[3]
306LTKVWPHKDYPLIPVubiquitination[1]
315YPLIPVGKLVLNKNPacetylation[2, 3]
315YPLIPVGKLVLNKNPsuccinylation[3]
315YPLIPVGKLVLNKNPubiquitination[1]
349GIEPSPDKMLQGRLFubiquitination[1]
430VQCAVDVKRFNSANEacetylation[2, 3, 4, 5, 6, 7]
430VQCAVDVKRFNSANEsuccinylation[3]
430VQCAVDVKRFNSANEubiquitination[1]
449QVRTFYTKVLNEEERacetylation[2, 3, 4, 5, 6, 7, 8, 9, 10]
449QVRTFYTKVLNEEERsuccinylation[3]
449QVRTFYTKVLNEEERubiquitination[1]
468ENIAGHLKDAQLFIQubiquitination[1]
476DAQLFIQKKAVKNFTacetylation[2]
476DAQLFIQKKAVKNFTubiquitination[1]
480FIQKKAVKNFTDVHPacetylation[2]
480FIQKKAVKNFTDVHPubiquitination[1]
499RIQALLDKYNAEKPKacetylation[2]
499RIQALLDKYNAEKPKubiquitination[1]
504LDKYNAEKPKNAIHTacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [9] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [10] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
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. 
Sequence Annotation
 ACT_SITE 75 75 By similarity.
 ACT_SITE 148 148 By similarity.
 METAL 358 358 Iron (heme axial ligand) (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 422 422 Phosphoserine.
 MOD_RES 517 517 Phosphoserine.  
Keyword
 Acetylation; 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
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE 60
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVTGES 120
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD 180
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ 240
GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT 300
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD 360
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE 420
HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK 480
NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL 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:0005739; C:mitochondrion; IDA:MGI.
 GO:0005778; C:peroxisomal membrane; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004046; F:aminoacylase activity; IMP:MGI.
 GO:0004096; F:catalase activity; IDA:MGI.
 GO:0020037; F:heme binding; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050661; F:NADP binding; IEA:Compara.
 GO:0009060; P:aerobic respiration; IMP:MGI.
 GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
 GO:0008203; P:cholesterol metabolic process; IMP:MGI.
 GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
 GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
 GO:0042697; P:menopause; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
 GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
 GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IDA:MGI.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 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; IMP:MGI.
 GO:0009650; P:UV protection; IEA:Compara. 
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.