ID KPRB_HUMAN Reviewed; 369 AA. AC O60256; B4E1M8; B7ZKZ1; E7EMY2; Q6IAS2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-OCT-2013, entry version 102. 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 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] (ISOFORM 1). RX 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] (ISOFORM 2). RC TISSUE=Trachea; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA] (ISOFORM 1). 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 [4] 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., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA 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 RT the human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). 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 [6] RP PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232; RP 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, AND RP MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; 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). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] 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., RA Buerckstuemmer T., 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS RP SPECTROMETRY. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369. RG Structural genomics consortium (SGC); RT "Human phosphoribosylpyrophosphate synthetase-associated protein 41 RT (Pap41)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Seems to play a negative regulatory role in 5- CC phosphoribose 1-diphosphate synthesis. CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O60256-1; Sequence=Displayed; CC Name=2; CC IsoId=O60256-2; Sequence=VSP_044731; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=O60256-3; Sequence=VSP_046462; CC Note=No experimental confirmation available; 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; AK303911; BAG64840.1; -; mRNA. DR EMBL; CR457082; CAG33363.1; -; mRNA. DR EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC106050; AAI06051.1; -; mRNA. DR EMBL; BC101670; AAI01671.1; -; mRNA. DR EMBL; BC101672; AAI01673.1; -; mRNA. DR EMBL; BC143475; AAI43476.1; -; mRNA. DR IPI; IPI00003168; -. DR IPI; IPI00796213; -. DR IPI; IPI00942171; -. DR RefSeq; NP_001230865.1; NM_001243936.1. DR RefSeq; NP_001230869.1; NM_001243940.1. DR RefSeq; NP_001230870.1; NM_001243941.1. DR RefSeq; NP_001230871.1; NM_001243942.1. DR RefSeq; NP_002758.1; NM_002767.3. DR UniGene; Hs.632236; -. DR PDB; 2JI4; X-ray; 2.55 A; A=13-369. DR PDBsum; 2JI4; -. DR ProteinModelPortal; O60256; -. DR SMR; O60256; 19-368. DR IntAct; O60256; 1. DR MINT; MINT-5003869; -. DR STRING; 9606.ENSP00000268835; -. DR PhosphoSite; O60256; -. DR PaxDb; O60256; -. DR PeptideAtlas; O60256; -. DR PRIDE; O60256; -. DR Ensembl; ENST00000268835; ENSP00000268835; ENSG00000141127. DR Ensembl; ENST00000419071; ENSP00000392536; ENSG00000141127. DR Ensembl; ENST00000542013; ENSP00000439129; ENSG00000141127. DR GeneID; 5636; -. DR KEGG; hsa:5636; -. DR UCSC; uc010vyi.2; human. DR CTD; 5636; -. DR GeneCards; GC17P018702; -. DR HGNC; HGNC:9467; PRPSAP2. DR HPA; HPA021881; -. DR MIM; 603762; gene. DR neXtProt; NX_O60256; -. DR PharmGKB; PA33822; -. DR eggNOG; COG0462; -. DR HOGENOM; HOG000210451; -. DR HOVERGEN; HBG001520; -. DR InParanoid; O60256; -. DR OMA; KLLAKMM; -. DR PhylomeDB; O60256; -. DR BindingDB; O60256; -. DR ChEMBL; CHEMBL2646; -. DR ChiTaRS; PRPSAP2; human. DR EvolutionaryTrace; O60256; -. DR GeneWiki; PRPSAP2; -. DR GenomeRNAi; 5636; -. DR NextBio; 21902; -. DR PRO; PR:O60256; -. DR ArrayExpress; O60256; -. DR Bgee; O60256; -. DR CleanEx; HS_PRPSAP2; -. DR Genevestigator; O60256; -. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl. DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Nucleotide biosynthesis; Phosphoprotein; KW Reference proteome. FT CHAIN 1 369 Phosphoribosyl pyrophosphate synthase- FT associated protein 2. FT /FTId=PRO_0000141082. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 227 227 Phosphoserine. FT VAR_SEQ 41 80 Missing (in isoform 2). FT /FTId=VSP_044731. FT VAR_SEQ 269 317 Missing (in isoform 3). FT /FTId=VSP_046462. FT CONFLICT 121 121 K -> R (in Ref. 2; BAG64840). FT STRAND 21 24 FT HELIX 29 32 FT HELIX 33 42 FT STRAND 49 53 FT STRAND 59 63 FT STRAND 71 75 FT HELIX 82 98 FT STRAND 102 107 FT HELIX 126 136 FT STRAND 141 146 FT HELIX 150 155 FT STRAND 156 158 FT STRAND 160 163 FT HELIX 166 176 FT HELIX 180 182 FT STRAND 183 189 FT HELIX 190 192 FT HELIX 193 202 FT STRAND 206 210 FT STRAND 256 258 FT STRAND 263 272 FT HELIX 276 287 FT STRAND 292 300 FT HELIX 306 312 FT STRAND 317 324 FT HELIX 327 331 FT STRAND 336 339 FT HELIX 342 354 FT STRAND 362 364 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 //