ID KPRB_HUMAN Reviewed; 369 AA. AC O60256; Q6IAS2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 06-FEB-2007, entry version 36. DE Phosphoribosyl pyrophosphate synthetase-associated protein 2 (PRPP DE synthetase-associated protein 2) (41 kDa phosphoribosypyrophosphate DE synthetase-associated protein) (PAP41). GN Name=PRPSAP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98207714; PubMed=9545573; DOI=10.1016/S0167-4781(97)00217-0; RA Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T., RA Tatibana M., Itakura M.; RT "Molecular cloning of a human cDNA for the 41-kDa RT phosphoribosylpyrophosphate synthetase-associated protein."; RL Biochim. Biophys. Acta 1396:245-250(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). CC -!- FUNCTION: Seems to play a negative regulatory role in PRPP CC synthesis. CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB007851; BAA25435.1; -; mRNA. DR EMBL; CR457082; CAG33363.1; -; mRNA. DR EMBL; BC106050; AAI06051.1; -; mRNA. DR EMBL; BC101670; AAI01671.1; -; mRNA. DR EMBL; BC101672; AAI01673.1; -; mRNA. DR UniGene; Hs.462418; -. DR HSSP; P14193; 1DKR. DR SMR; O60256; 19-363. DR Ensembl; ENSG00000141127; Homo sapiens. DR KEGG; hsa:5636; -. DR HGNC; HGNC:9467; PRPSAP2. DR MIM; 603762; gene. DR ArrayExpress; O60256; -. DR GermOnline; ENSG00000141127; Homo sapiens. DR RZPD-ProtExp; IOH26183; -. DR RZPD-ProtExp; RZPDo834E0144; -. DR RZPD-ProtExp; RZPDo834G0711; -. DR RZPD-ProtExp; S0019; -. DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc. DR GO; GO:0006139; P:nucleobase, nucleoside, nucleotide and nucl...; TAS:ProtInc. DR InterPro; IPR000836; PRtransferase. DR InterPro; IPR007337; RelB. DR InterPro; IPR005946; RibP_Ppkin. DR Pfam; PF00156; Pribosyltran; 1. DR Pfam; PF04221; RelB; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. KW Nucleotide biosynthesis; Phosphorylation. FT CHAIN 1 369 Phosphoribosyl pyrophosphate synthetase- FT associated protein 2. FT /FTId=PRO_0000141082. FT MOD_RES 227 227 Phosphoserine. SQ SEQUENCE 369 AA; 40926 MW; 12A0E46BD4AC55BF CRC64; MFCVTPPELE 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 LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY LFRNIGLDD //