UniProt Accession

 KPRA_HUMAN; Q14558; B2R6M4; Q96H06 

Genbank Protein ID

 D61391; AK312637; AC090699; CH471099; BC009012 

Genbank Nucleotide ID

 BAA09612.1; BAG35521.1; EAW89386.1; AAH09012.1 

Protein Name

 Phosphoribosyl pyrophosphate synthase-associated protein 1 

Protein Synonyms/Alias

 PRPP synthase-associated protein 1; 39 kDa phosphoribosypyrophosphate synthase-associated protein; PAP39 

Gene Name

 PRPSAP1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
24	AACTELAKRITERLG	ubiquitination	[1, 2]
36	RLGAELGKSVVYQET	ubiquitination	[3]
176	RNAVIVAKSPDAAKR	ubiquitination	[3]
238	PLMMAKEKPPITVVG	ubiquitination	[3]

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] 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]
 [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] 

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 215 215 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Nucleotide biosynthesis; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 356 AA 

Protein Sequence

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:0033673; P:negative regulation of kinase activity; IEA:Compara.
 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