KPRA_HUMAN
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 03-AUG-2022, entry version 184.
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; 109.
DR IntAct; Q14558; 48.
DR MINT; Q14558; -.
DR STRING; 9606.ENSP00000414624; -.
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; Q14558; -.
DR PeptideAtlas; Q14558; -.
DR PRIDE; Q14558; -.
DR ProteomicsDB; 60042; -. [Q14558-1]
DR ProteomicsDB; 60043; -. [Q14558-2]
DR Antibodypedia; 32394; 186 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 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; CHELKIF; -.
DR OrthoDB; 1043963at2759; -.
DR PhylomeDB; Q14558; -.
DR TreeFam; TF106367; -.
DR PathwayCommons; Q14558; -.
DR SignaLink; Q14558; -.
DR BioGRID-ORCS; 5635; 7 hits in 1074 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 203 other tissues.
DR ExpressionAtlas; Q14558; baseline and differential.
DR Genevisible; Q14558; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; 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 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 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
