CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003980
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribose-phosphate pyrophosphokinase 2 
Protein Synonyms/Alias
 PPRibP; Phosphoribosyl pyrophosphate synthase II; PRS-II 
Gene Name
 PRPS2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
179SPDAGGAKRVTSIADubiquitination[1]
215MVLVGDVKDRVAILVubiquitination[2, 3]
283NTIPQEDKMKHCTKIubiquitination[1]
285IPQEDKMKHCTKIQVubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. 
Sequence Annotation
 NP_BIND 96 101 ATP (By similarity).
 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 (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 318 AA 
Protein Sequence
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC 60
GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKVGESRAPI SAKLVANMLS 120
VAGADHIITM DLHASQIQGF FDIPVDNLYA EPAVLQWIRE NIAEWKNCII VSPDAGGAKR 180
VTSIADRLNV EFALIHKERK KANEVDRMVL VGDVKDRVAI LVDDMADTCG TICHAADKLL 240
SAGATKVYAI LTHGIFSGPA ISRINNAAFE AVVVTNTIPQ EDKMKHCTKI QVIDISMILA 300
EAIRRTHNGE SVSYLFSHVP L 321 
Gene Ontology
 GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Compara.
 GO:0043531; F:ADP binding; IEA:Compara.
 GO:0016208; F:AMP binding; IEA:Compara.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0030246; F:carbohydrate binding; IEA:Compara.
 GO:0019003; F:GDP binding; IEA:Compara.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006167; P:AMP biosynthetic process; IEA:Compara.
 GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO:0031100; P:organ regeneration; IEA:Compara. 
Interpro
 IPR000842; PRib_PP_synth_CS.
 IPR000836; PRibTrfase_dom.
 IPR005946; Rib-P_diPkinase. 
Pfam
 PF00156; Pribosyltran 
SMART
  
PROSITE
 PS00114; PRPP_SYNTHASE 
PRINTS