CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002533
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenine phosphoribosyltransferase 
Protein Synonyms/Alias
 APRT 
Gene Name
 APRT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34RDISPVLKDPASFRAubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
114KAELEIQKDALEPGQacetylation[9]
114KAELEIQKDALEPGQubiquitination[2, 6, 7]
167TSLKGREKLAPVPFFubiquitination[2, 6, 7]
Reference
 [1] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] 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]
 [9] 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
Functional Description
 Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 60 60 Phosphotyrosine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 114 114 N6-acetyllysine.
 MOD_RES 135 135 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycosyltransferase; Phosphoprotein; Polymorphism; Purine salvage; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 180 AA 
Protein Sequence
MADSELQLVE QRIRSFPDFP TPGVVFRDIS PVLKDPASFR AAIGLLARHL KATHGGRIDY 60
IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTLWAS YSLEYGKAEL EIQKDALEPG 120
QRVVVVDDLL ATGGTMNAAC ELLGRLQAEV LECVSLVELT SLKGREKLAP VPFFSLLQYE 180 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0002055; F:adenine binding; IEA:Compara.
 GO:0003999; F:adenine phosphoribosyltransferase activity; TAS:Reactome.
 GO:0016208; F:AMP binding; IDA:MGI.
 GO:0006168; P:adenine salvage; IEA:Compara.
 GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0007625; P:grooming behavior; IEA:Compara.
 GO:0007595; P:lactation; IEA:Compara.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
 GO:0043101; P:purine-containing compound salvage; TAS:Reactome. 
Interpro
 IPR005764; Ade_phspho_trans.
 IPR000836; PRibTrfase_dom. 
Pfam
 PF00156; Pribosyltran 
SMART
  
PROSITE
 PS00103; PUR_PYR_PR_TRANSFER 
PRINTS