UniProt Accession

 PRPS2_HUMAN; P11908; Q0VDH9; Q0VDI0; Q15245; Q2TAK7 

Genbank Protein ID

 Y00971; BC030019; BC040483; BC110875; BC119662; BC119663; D28134 

Genbank Nucleotide ID

 CAA68785.1; AAH30019.2; AAH40483.3; AAI10876.2; AAI19663.1; AAI19664.1; BAA05676.1 

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
29	RLGLELGKVVTKKFS	ubiquitination	[1]
34	LGKVVTKKFSNQETS	ubiquitination	[2]
176	SPDAGGAKRVTSIAD	ubiquitination	[3]
194	VEFALIHKERKKANE	acetylation	[4]
212	MVLVGDVKDRVAILV	ubiquitination	[1]
280	NTIPQEDKMKHCTKI	ubiquitination	[1]

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] 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]
 [3] 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]
 [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] 

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

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