CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005441
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uricase 
Protein Synonyms/Alias
 Urate oxidase 
Gene Name
 Uox 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
10HYHDNYGKNDEVEFVacetylation[1, 2, 3, 4, 5]
10HYHDNYGKNDEVEFVsuccinylation[4]
10HYHDNYGKNDEVEFVubiquitination[6]
23FVRTGYGKDMVKVLHacetylation[2, 3, 4, 5]
23FVRTGYGKDMVKVLHsuccinylation[4]
23FVRTGYGKDMVKVLHubiquitination[6]
27GYGKDMVKVLHIQRDacetylation[2, 3]
27GYGKDMVKVLHIQRDubiquitination[6]
36LHIQRDGKYHSIKEVacetylation[1, 2, 3, 5, 7, 8]
54VQLTLRSKKDYLHGDacetylation[3]
55QLTLRSKKDYLHGDNacetylation[7]
55QLTLRSKKDYLHGDNubiquitination[6]
72IIPTDTIKNTVHVLAacetylation[2, 5]
72IIPTDTIKNTVHVLAubiquitination[6]
80NTVHVLAKLRGIRNIacetylation[2, 4, 5]
80NTVHVLAKLRGIRNIsuccinylation[4]
80NTVHVLAKLRGIRNIubiquitination[6]
118YVEEVPWKRFEKNGIacetylation[2, 7]
118YVEEVPWKRFEKNGIubiquitination[6]
122VPWKRFEKNGIKHVHacetylation[2, 7]
126RFEKNGIKHVHAFIHacetylation[2]
158PVIHSGIKDLKVLKTacetylation[2]
158PVIHSGIKDLKVLKTubiquitination[6]
161HSGIKDLKVLKTTQSacetylation[2]
164IKDLKVLKTTQSGFEacetylation[7]
164IKDLKVLKTTQSGFEubiquitination[6]
175SGFEGFLKDQFTTLPacetylation[2]
175SGFEGFLKDQFTTLPubiquitination[6]
185FTTLPEVKDRCFATQacetylation[2, 7]
185FTTLPEVKDRCFATQubiquitination[6]
196FATQVYCKWRYQRRDacetylation[2]
196FATQVYCKWRYQRRDubiquitination[6]
220VRDIVLQKFAGPYDKacetylation[2, 7]
220VRDIVLQKFAGPYDKubiquitination[6]
227KFAGPYDKGEYSPSVacetylation[2, 7]
227KFAGPYDKGEYSPSVubiquitination[6]
277SKMGLINKEEVLLPLacetylation[1, 2, 3, 4, 5, 7, 8]
277SKMGLINKEEVLLPLsuccinylation[4]
290PLDNPYGKITGTVKRacetylation[1, 4, 5, 7]
290PLDNPYGKITGTVKRsuccinylation[4]
296GKITGTVKRKLPSRLacetylation[3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] 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
Functional Description
 Catalyzes the oxidation of uric acid to 5- hydroxyisourate, which is further processed to form (S)-allantoin. 
Sequence Annotation
 REGION 68 69 Substrate binding (By similarity).
 REGION 234 235 Substrate binding (By similarity).
 MOTIF 301 303 Microbody targeting signal (Potential).
 ACT_SITE 187 187 Charge relay system (By similarity).
 ACT_SITE 235 235 Charge relay system (By similarity).
 BINDING 187 187 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 36 36 N6-acetyllysine.
 MOD_RES 39 39 Phosphoserine.
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 118 118 N6-acetyllysine.
 MOD_RES 122 122 N6-acetyllysine.
 MOD_RES 164 164 N6-acetyllysine.
 MOD_RES 185 185 N6-acetyllysine.
 MOD_RES 220 220 N6-acetyllysine.
 MOD_RES 227 227 N6-acetyllysine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 277 277 N6-acetyllysine.
 MOD_RES 290 290 N6-acetyllysine.
 MOD_RES 301 301 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Oxidoreductase; Peroxisome; Phosphoprotein; Purine metabolism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 303 AA 
Protein Sequence
MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LRSKKDYLHG 60
DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS SFNHVTRAHV YVEEVPWKRF 120
EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT 180
LPEVKDRCFA TQVYCKWRYQ RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD 240
IQVLSLSQLP EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP 300
SRL 303 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005777; C:peroxisome; TAS:MGI.
 GO:0004846; F:urate oxidase activity; TAS:MGI.
 GO:0006144; P:purine nucleobase metabolic process; TAS:MGI.
 GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR002042; Uricase.
 IPR019842; Uricase_CS. 
Pfam
 PF01014; Uricase 
SMART
  
PROSITE
 PS00366; URICASE 
PRINTS
 PR00093; URICASE.