CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003886
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uridine 5'-monophosphate synthase 
Protein Synonyms/Alias
 UMP synthase; Orotate phosphoribosyltransferase; OPRT; OPRTase; Orotidine 5'-phosphate decarboxylase; ODC; OMPdecase 
Gene Name
 UMPS 
Gene Synonyms/Alias
 OK/SW-cl.21 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22LYDVQAFKFGDFVLKubiquitination[1]
29KFGDFVLKSGLSSPIubiquitination[1]
160LDREQGGKDKLQAHGubiquitination[2]
162REQGGKDKLQAHGIRacetylation[3]
162REQGGKDKLQAHGIRubiquitination[2]
178HSVCTLSKMLEILEQubiquitination[2]
187LEILEQQKKVDAETVubiquitination[2]
188EILEQQKKVDAETVGubiquitination[2]
219NGSPLSIKEAPKELSubiquitination[1, 2]
223LSIKEAPKELSFGARubiquitination[2]
242RIHPVASKLLRLMQKubiquitination[2]
314FLIFEDRKFADIGNTubiquitination[1, 2]
323ADIGNTVKKQYEGGIubiquitination[1, 2]
324DIGNTVKKQYEGGIFubiquitination[1, 2, 4]
332QYEGGIFKIASWADLubiquitination[2]
352VPGSGVVKGLQEVGLubiquitination[2]
409SGSRVSMKPEFLHLTubiquitination[1, 2]
441SPQEVIGKRGSDIIIubiquitination[1, 5]
468EAAEMYRKAAWEAYLubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
 REGION 2 214 OPRTase.
 REGION 215 220 Domain linker.
 REGION 221 480 OMPdecase.
 ACT_SITE 312 312 For OMPdecase activity.
 ACT_SITE 314 314 For OMPdecase activity.
 ACT_SITE 317 317 For OMPdecase activity.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 214 214 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Decarboxylase; Disease mutation; Glycosyltransferase; Lyase; Multifunctional enzyme; Phosphoprotein; Polymorphism; Pyrimidine biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 480 AA 
Protein Sequence
MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT 60
AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL 120
IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML 180
EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA 240
SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT 300
LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP 360
LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ 420
LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV 480 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:UniProtKB.
 GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IDA:UniProtKB.
 GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
 GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0035690; P:cellular response to drug; IEA:Compara.
 GO:0007565; P:female pregnancy; IEA:Compara.
 GO:0007595; P:lactation; IEA:Compara.
 GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
 GO:0006222; P:UMP biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR014732; OMPdecase.
 IPR018089; OMPdecase_AS.
 IPR001754; OMPdeCOase_dom.
 IPR023031; OPRT.
 IPR004467; Or_phspho_trans_dom.
 IPR000836; PRibTrfase_dom.
 IPR011060; RibuloseP-bd_barrel. 
Pfam
 PF00215; OMPdecase
 PF00156; Pribosyltran 
SMART
 SM00934; OMPdecase 
PROSITE
 PS00156; OMPDECASE
 PS00103; PUR_PYR_PR_TRANSFER 
PRINTS