KPRA_MOUSE
ID KPRA_MOUSE Reviewed; 356 AA.
AC Q9D0M1;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 1;
DE Short=PRPP synthase-associated protein 1;
DE AltName: Full=39 kDa phosphoribosypyrophosphate synthase-associated protein;
DE Short=PAP39;
GN Name=Prpsap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose
CC 1-diphosphate synthesis. {ECO:0000250}.
CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AK011290; BAB27520.1; -; mRNA.
DR EMBL; BC029621; AAH29621.1; -; mRNA.
DR RefSeq; NP_080640.1; NM_026364.1.
DR AlphaFoldDB; Q9D0M1; -.
DR SMR; Q9D0M1; -.
DR BioGRID; 212425; 9.
DR DIP; DIP-59971N; -.
DR IntAct; Q9D0M1; 1.
DR STRING; 10090.ENSMUSP00000101999; -.
DR iPTMnet; Q9D0M1; -.
DR PhosphoSitePlus; Q9D0M1; -.
DR EPD; Q9D0M1; -.
DR jPOST; Q9D0M1; -.
DR MaxQB; Q9D0M1; -.
DR PaxDb; Q9D0M1; -.
DR PeptideAtlas; Q9D0M1; -.
DR PRIDE; Q9D0M1; -.
DR ProteomicsDB; 263561; -.
DR DNASU; 67763; -.
DR GeneID; 67763; -.
DR KEGG; mmu:67763; -.
DR CTD; 5635; -.
DR MGI; MGI:1915013; Prpsap1.
DR eggNOG; KOG1503; Eukaryota.
DR InParanoid; Q9D0M1; -.
DR OrthoDB; 1043963at2759; -.
DR BioGRID-ORCS; 67763; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Prpsap1; mouse.
DR PRO; PR:Q9D0M1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D0M1; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; ISO:MGI.
DR GO; GO:0030234; F:enzyme regulator activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
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:0033673; P:negative regulation of kinase activity; ISO:MGI.
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..356
FT /note="Phosphoribosyl pyrophosphate synthase-associated
FT protein 1"
FT /id="PRO_0000141080"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14558"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14558"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 356 AA; 39432 MW; 0BCEA75BFE55401E CRC64;
MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE IKESVRGQDI
FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP YSKQSKMRKR GSIVCKLLAS
MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN LRASPFLLQY IQEEIPNYRN AVIVAKSPDA
AKRAQSYAER LRLGLAVIHG EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP
ITVVGDVGGR IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES
PIDEVVVTNT VPHELQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR NITVDD
