CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009266
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribose-phosphate pyrophosphokinase 1 
Protein Synonyms/Alias
 PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I 
Gene Name
 PRPS1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MPNIKIFSGSSHubiquitination[1, 2]
18SHQDLSQKIADRLGLubiquitination[1, 2]
29RLGLELGKVVTKKFSubiquitination[1, 2]
176SPDAGGAKRVTSIADubiquitination[2, 3]
194VDFALIHKERKKANEubiquitination[1, 2, 3]
212MVLVGDVKDRVAILVubiquitination[1, 2, 3, 4]
235TICHAADKLLSAGATubiquitination[2]
280NTIPQEDKMKHCSKIubiquitination[2]
282IPQEDKMKHCSKIQVubiquitination[2]
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] 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] 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]
 [4] 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] 
Functional Description
 Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. 
Sequence Annotation
 NP_BIND 96 101 ATP.
 REGION 212 227 Binding of phosphoribosylpyrophosphate
 METAL 128 128 Magnesium (Potential).
 METAL 130 130 Magnesium (Potential).
 METAL 139 139 Magnesium (Potential).
 METAL 143 143 Magnesium (Potential).
 BINDING 130 130 ATP.  
Keyword
 3D-structure; ATP-binding; Charcot-Marie-Tooth disease; Complete proteome; Deafness; Direct protein sequencing; Disease mutation; Gout; Kinase; Magnesium; Mental retardation; Metal-binding; Neuropathy; Non-syndromic deafness; Nucleotide biosynthesis; Nucleotide-binding; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 318 AA 
Protein Sequence
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC 60
GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG 120
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS 180
IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG 240
ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI 300
RRTHNGESVS YLFSHVPL 318 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004749; F:ribose phosphate diphosphokinase activity; IDA:UniProtKB.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; TAS:Reactome.
 GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
 GO:0046101; P:hypoxanthine biosynthetic process; IMP:UniProtKB.
 GO:0007399; P:nervous system development; IMP:UniProtKB.
 GO:0006164; P:purine nucleotide biosynthetic process; IMP:UniProtKB.
 GO:0006221; P:pyrimidine nucleotide biosynthetic process; NAS:UniProtKB.
 GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
 GO:0034418; P:urate biosynthetic process; IMP:UniProtKB. 
Interpro
 IPR000842; PRib_PP_synth_CS.
 IPR000836; PRibTrfase_dom.
 IPR005946; Rib-P_diPkinase. 
Pfam
 PF00156; Pribosyltran 
SMART
  
PROSITE
 PS00114; PRPP_SYNTHASE 
PRINTS