CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006245
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribose-phosphate pyrophosphokinase 1 
Protein Synonyms/Alias
 Phosphoribosyl pyrophosphate synthase 1 
Gene Name
 PRS1 
Gene Synonyms/Alias
 PPS1; PRP1; PRPS; PRPS1; YKL181W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
5***MRKCKIFVGNSHubiquitination[1]
96IPQFPYSKQCKMKRHacetylation[2]
170EDAVVVSKNPGGTKRubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1- diphosphate synthases (PRS2, PRS3, PRS4 and PRS5). 
Sequence Annotation
 METAL 128 128 Magnesium (Potential).
 METAL 130 130 Magnesium (Potential).
 METAL 143 143 Magnesium (Potential).
 MOD_RES 199 199 Phosphoserine.
 MOD_RES 218 218 Phosphoserine.
 MOD_RES 271 271 Phosphoserine.
 MOD_RES 295 295 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 427 AA 
Protein Sequence
MRKCKIFVGN SHPELGNMVC QRLGIEPAPC TLKKFANGET SVQIGVSVRD EDVYVIQSGS 60
PSINDDIMEL LILVSACRGG SARKITAVIP QFPYSKQCKM KRHRGAITAR MLANLLVMAG 120
ADHVVSMDLH ASQMQGFFTK PVDNLYGGPS LAKWIRENVE DYEDAVVVSK NPGGTKRVTA 180
LADSLKINFA MIHTDRRRSK DLYSQNKDLQ QLKLRKQSML RKNRPIIRQG DHPNEEENII 240
LSNGIQTARI RNGHVIGDDE ADDDEDAILE SDSELHSIDG LDSHGLGGTY DAVDSEDEEE 300
IPVLYREQLI TLVGNVRGRS AIILDDMIDR PGSFISAAEH LVQNCGAKKV YVVATHGIFT 360
GDCLEELEKS DAIDTIVVTN TYPISGERIA GSKKLVTIDV SPIFAECIRR DHYGESISVL 420
FDSLAAL 427 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:EC.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IMP:SGD.
 GO:0031505; P:fungal-type cell wall organization; IPI:SGD.
 GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
 GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro. 
Interpro
 IPR000842; PRib_PP_synth_CS.
 IPR005946; Rib-P_diPkinase. 
Pfam
  
SMART
  
PROSITE
 PS00114; PRPP_SYNTHASE 
PRINTS