ID   KPRB_RAT                Reviewed;         369 AA.
AC   O08618;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2;
DE            Short=PRPP synthase-associated protein 2;
DE   AltName: Full=41 kDa phosphoribosypyrophosphate synthetase-associated protein;
DE            Short=PAP41;
GN   Name=Prpsap2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9003449; DOI=10.1016/s0167-4781(96)00190-x;
RA   Sonoda T., Ishizuka T., Kita K., Ishijima S., Tatibana M.;
RT   "Cloning and sequencing of rat cDNA for the 41-kDa
RT   phosphoribosylpyrophosphate synthetase-associated protein has a high
RT   homology to the catalytic subunits and the 39-kDa associated protein.";
RL   Biochim. Biophys. Acta 1350:6-10(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose
CC       1-diphosphate synthesis.
CC   -!- SUBUNIT: Binds to PRPS1 and PRPS2.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; D84434; BAA19517.1; -; mRNA.
DR   RefSeq; NP_476472.1; NM_057131.1.
DR   RefSeq; XP_006246496.1; XM_006246434.3.
DR   RefSeq; XP_006246497.1; XM_006246435.3.
DR   RefSeq; XP_006246498.1; XM_006246436.3.
DR   RefSeq; XP_006246499.1; XM_006246437.3.
DR   RefSeq; XP_006246500.1; XM_006246438.3.
DR   AlphaFoldDB; O08618; -.
DR   SMR; O08618; -.
DR   BioGRID; 250719; 2.
DR   IntAct; O08618; 2.
DR   STRING; 10116.ENSRNOP00000003697; -.
DR   iPTMnet; O08618; -.
DR   PhosphoSitePlus; O08618; -.
DR   jPOST; O08618; -.
DR   PaxDb; O08618; -.
DR   PRIDE; O08618; -.
DR   Ensembl; ENSRNOT00000003697; ENSRNOP00000003697; ENSRNOG00000002724.
DR   GeneID; 117272; -.
DR   KEGG; rno:117272; -.
DR   UCSC; RGD:620207; rat.
DR   CTD; 5636; -.
DR   RGD; 620207; Prpsap2.
DR   eggNOG; KOG1503; Eukaryota.
DR   GeneTree; ENSGT00950000182803; -.
DR   InParanoid; O08618; -.
DR   OMA; HYAYARS; -.
DR   OrthoDB; 1043963at2759; -.
DR   PhylomeDB; O08618; -.
DR   TreeFam; TF106367; -.
DR   SABIO-RK; O08618; -.
DR   PRO; PR:O08618; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002724; Expressed in thymus and 20 other tissues.
DR   ExpressionAtlas; O08618; baseline and differential.
DR   Genevisible; O08618; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0060348; P:bone development; ISO:RGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   PANTHER; PTHR10210; PTHR10210; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleotide biosynthesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Phosphoribosyl pyrophosphate synthase-associated
FT                   protein 2"
FT                   /id="PRO_0000141084"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O60256"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60256"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60256"
SQ   SEQUENCE   369 AA;  40867 MW;  E7436F13F1D34F0B CRC64;
     MFCVAPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
     VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
     KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
     RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
     LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
     LLSSDAPRLI EESAIDEVVV TNTIPHEIQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
     LFRNIGLDD