CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000894
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoribosyl pyrophosphate synthase-associated protein 2 
Protein Synonyms/Alias
 PRPP synthase-associated protein 2; 41 kDa phosphoribosypyrophosphate synthetase-associated protein; PAP41 
Gene Name
 PRPSAP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115IPYFPYSKQCKMRKRubiquitination[1]
188RNAVIVAKSPASAKRubiquitination[2]
251PMLIPKEKPPITVVGacetylation[3]
251PMLIPKEKPPITVVGubiquitination[1, 2, 4, 5]
335VQKLQCPKIKTVDISubiquitination[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] 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] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Seems to play a negative regulatory role in 5- phosphoribose 1-diphosphate synthesis. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 227 227 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Nucleotide biosynthesis; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 369 AA 
Protein Sequence
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR 60
VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR 120
KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY 180
RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS 240
LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG 300
LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY 360
LFRNIGLDD 369 
Gene Ontology
 GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Compara.
 GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
 GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR005946; Rib-P_diPkinase. 
Pfam
  
SMART
  
PROSITE
  
PRINTS