ID KPRA_HUMAN Reviewed; 356 AA. AC Q14558; B2R6M4; Q96H06; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 2. DT 27-MAR-2024, entry version 193. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hepatoma; RX PubMed=8611620; DOI=10.1016/0167-4781(96)00030-9; RA Ishizuka T., Kita K., Sonoda T., Ishijima S., Sawa K., Suzuki N., RA Tatibana M.; RT "Cloning and sequencing of human complementary DNA for the RT phosphoribosylpyrophosphate synthetase-associated protein 39."; RL Biochim. Biophys. Acta 1306:27-30(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2). RC TISSUE=Brain; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 5-361. RG Structural genomics consortium (SGC); RT "Crystal structure of human phosphoribosylpyrophosphate synthetase- RT associated protein 39 (Pap39)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose CC 1-diphosphate synthesis. CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. CC -!- INTERACTION: CC Q14558; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-724449, EBI-1765641; CC Q14558; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-724449, EBI-746778; CC Q14558; P60891: PRPS1; NbExp=11; IntAct=EBI-724449, EBI-749195; CC Q14558; P11908: PRPS2; NbExp=5; IntAct=EBI-724449, EBI-4290895; CC Q14558; P11908-2: PRPS2; NbExp=3; IntAct=EBI-724449, EBI-12063547; CC Q14558; Q14558: PRPSAP1; NbExp=5; IntAct=EBI-724449, EBI-724449; CC Q14558; O60256: PRPSAP2; NbExp=6; IntAct=EBI-724449, EBI-724960; CC Q14558; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-724449, EBI-10180829; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14558-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14558-2; Sequence=VSP_039062; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG35521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; D61391; BAA09612.1; -; mRNA. DR EMBL; AK312637; BAG35521.1; ALT_INIT; mRNA. DR EMBL; AC090699; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89386.1; -; Genomic_DNA. DR EMBL; BC009012; AAH09012.1; -; mRNA. DR CCDS; CCDS11743.2; -. [Q14558-2] DR PIR; S71460; S71460. DR RefSeq; NP_002757.2; NM_002766.2. [Q14558-2] DR PDB; 2C4K; X-ray; 2.65 A; A/B/C/D/E/F=5-351. DR PDBsum; 2C4K; -. DR AlphaFoldDB; Q14558; -. DR SMR; Q14558; -. DR BioGRID; 111618; 124. DR IntAct; Q14558; 50. DR MINT; Q14558; -. DR STRING; 9606.ENSP00000414624; -. DR GlyGen; Q14558; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q14558; -. DR PhosphoSitePlus; Q14558; -. DR BioMuta; PRPSAP1; -. DR DMDM; 24418495; -. DR EPD; Q14558; -. DR jPOST; Q14558; -. DR MassIVE; Q14558; -. DR MaxQB; Q14558; -. DR PaxDb; 9606-ENSP00000414624; -. DR PeptideAtlas; Q14558; -. DR ProteomicsDB; 60042; -. [Q14558-1] DR ProteomicsDB; 60043; -. [Q14558-2] DR Pumba; Q14558; -. DR Antibodypedia; 32394; 210 antibodies from 27 providers. DR DNASU; 5635; -. DR Ensembl; ENST00000446526.8; ENSP00000414624.2; ENSG00000161542.17. [Q14558-2] DR GeneID; 5635; -. DR KEGG; hsa:5635; -. DR MANE-Select; ENST00000446526.8; ENSP00000414624.2; NM_002766.3; NP_002757.2. [Q14558-2] DR UCSC; uc010wta.2; human. [Q14558-1] DR AGR; HGNC:9466; -. DR CTD; 5635; -. DR DisGeNET; 5635; -. DR GeneCards; PRPSAP1; -. DR HGNC; HGNC:9466; PRPSAP1. DR HPA; ENSG00000161542; Low tissue specificity. DR MIM; 601249; gene. DR neXtProt; NX_Q14558; -. DR OpenTargets; ENSG00000161542; -. DR PharmGKB; PA33821; -. DR VEuPathDB; HostDB:ENSG00000161542; -. DR eggNOG; KOG1503; Eukaryota. DR GeneTree; ENSGT00950000182803; -. DR InParanoid; Q14558; -. DR OMA; GIIACPG; -. DR OrthoDB; 276387at2759; -. DR PhylomeDB; Q14558; -. DR TreeFam; TF106367; -. DR PathwayCommons; Q14558; -. DR SignaLink; Q14558; -. DR BioGRID-ORCS; 5635; 9 hits in 1152 CRISPR screens. DR ChiTaRS; PRPSAP1; human. DR EvolutionaryTrace; Q14558; -. DR GeneWiki; PRPSAP1; -. DR GenomeRNAi; 5635; -. DR Pharos; Q14558; Tbio. DR PRO; PR:Q14558; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q14558; Protein. DR Bgee; ENSG00000161542; Expressed in parotid gland and 205 other cell types or tissues. DR ExpressionAtlas; Q14558; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.2020; -; 2. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR NCBIfam; TIGR01251; ribP_PPkin; 1. DR PANTHER; PTHR10210:SF28; PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SMART; SM01400; Pribosyltran_N; 1. DR SUPFAM; SSF53271; PRTase-like; 2. DR Genevisible; Q14558; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Nucleotide biosynthesis; KW Phosphoprotein; Reference proteome. FT CHAIN 1..356 FT /note="Phosphoribosyl pyrophosphate synthase-associated FT protein 1" FT /id="PRO_0000141079" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1 FT /note="M -> MPKKLLLLPPPSASSAFRVPRARPVPPPAM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039062" FT CONFLICT 12 FT /note="S -> L (in Ref. 1; BAA09612)" FT /evidence="ECO:0000305" FT CONFLICT 54 FT /note="S -> F (in Ref. 1; BAA09612)" FT /evidence="ECO:0000305" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:2C4K" FT TURN 17..20 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 21..29 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 70..86 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:2C4K" FT TURN 100..105 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 114..124 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 138..143 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 172..177 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 181..191 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 263..273 FT /evidence="ECO:0007829|PDB:2C4K" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 277..287 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 293..299 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 314..319 FT /evidence="ECO:0007829|PDB:2C4K" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 329..341 FT /evidence="ECO:0007829|PDB:2C4K" FT HELIX 346..349 FT /evidence="ECO:0007829|PDB:2C4K" SQ SEQUENCE 356 AA; 39394 MW; 38CC87AB2C555717 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 SVDEVVVTNT VPHEVQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR NITVDD //