PRPS2_HUMAN
ID PRPS2_HUMAN Reviewed; 318 AA.
AC P11908; Q0VDH9; Q0VDI0; Q15245; Q2TAK7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2;
DE EC=2.7.6.1;
DE AltName: Full=PPRibP;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase II;
DE Short=PRS-II;
GN Name=PRPS2;
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=Testis;
RX PubMed=2538352; DOI=10.1016/0014-5793(89)81159-7;
RA Iizasa T., Taira M., Shimada H., Ishijima S., Tatibana M.;
RT "Molecular cloning and sequencing of human cDNA for phosphoribosyl
RT pyrophosphate synthetase subunit II.";
RL FEBS Lett. 244:47-50(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=2560337; DOI=10.1007/978-1-4684-5673-8_84;
RA Iizasa T., Taira M., Shimada H., Tatibana M.;
RT "Deduced amino acid sequence from human phosphoribosylpyrophosphate
RT synthetase subunit II cDNA.";
RL Adv. Exp. Med. Biol. 253A:519-523(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC TISSUE=Leukocyte;
RX PubMed=1314091; DOI=10.1016/0167-4781(92)90521-z;
RA Ishizuka T., Iizasa T., Taira M., Ishijima S., Sonoda T., Shimada H.,
RA Nagatake N., Tatibana M.;
RT "Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2
RT encoding phosphoribosylpyrophosphate synthetase subunit I and II
RT isoforms.";
RL Biochim. Biophys. Acta 1130:139-148(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-29; 34-49; 85-96; 164-196; 205-214; 244-282 AND
RP 287-318, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Mammary carcinoma, and Osteosarcoma;
RA Bienvenut W.V., Calvo F., Bensaad K., Vousden K.H., Matallanas D.,
RA Cooper W.N., Kolch W., Lourenco F., Olson M.F.;
RL Submitted (DEC-2009) to UniProtKB.
RN [6]
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by magnesium and inorganic phosphate.
CC Competitively or non-competitively inhibited by ADP, 2,3-
CC bisphosphoglyceride or GDP.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3
CC homodimers (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P11908; P28799: GRN; NbExp=3; IntAct=EBI-4290895, EBI-747754;
CC P11908; P04792: HSPB1; NbExp=3; IntAct=EBI-4290895, EBI-352682;
CC P11908; O60333-2: KIF1B; NbExp=3; IntAct=EBI-4290895, EBI-10975473;
CC P11908; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-4290895, EBI-945833;
CC P11908; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-4290895, EBI-741158;
CC P11908; P60891: PRPS1; NbExp=10; IntAct=EBI-4290895, EBI-749195;
CC P11908; P11908: PRPS2; NbExp=4; IntAct=EBI-4290895, EBI-4290895;
CC P11908; Q14558: PRPSAP1; NbExp=5; IntAct=EBI-4290895, EBI-724449;
CC P11908; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-4290895, EBI-396669;
CC P11908; P02766: TTR; NbExp=3; IntAct=EBI-4290895, EBI-711909;
CC P11908; O76024: WFS1; NbExp=3; IntAct=EBI-4290895, EBI-720609;
CC P11908-2; P60891: PRPS1; NbExp=4; IntAct=EBI-12063547, EBI-749195;
CC P11908-2; Q14558: PRPSAP1; NbExp=3; IntAct=EBI-12063547, EBI-724449;
CC P11908-2; O60256: PRPSAP2; NbExp=4; IntAct=EBI-12063547, EBI-724960;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11908-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11908-2; Sequence=VSP_027769;
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30019.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y00971; CAA68785.1; -; mRNA.
DR EMBL; BC030019; AAH30019.2; ALT_INIT; mRNA.
DR EMBL; BC040483; AAH40483.3; -; mRNA.
DR EMBL; BC110875; AAI10876.2; -; mRNA.
DR EMBL; BC119662; AAI19663.1; -; mRNA.
DR EMBL; BC119663; AAI19664.1; -; mRNA.
DR EMBL; D28134; BAA05676.1; -; Genomic_DNA.
DR CCDS; CCDS14150.1; -. [P11908-1]
DR CCDS; CCDS43918.1; -. [P11908-2]
DR PIR; S02778; KIHUR2.
DR RefSeq; NP_001034180.1; NM_001039091.2. [P11908-2]
DR RefSeq; NP_002756.1; NM_002765.4. [P11908-1]
DR AlphaFoldDB; P11908; -.
DR SMR; P11908; -.
DR BioGRID; 111617; 218.
DR IntAct; P11908; 50.
DR MINT; P11908; -.
DR STRING; 9606.ENSP00000381504; -.
DR GlyGen; P11908; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11908; -.
DR MetOSite; P11908; -.
DR PhosphoSitePlus; P11908; -.
DR SwissPalm; P11908; -.
DR BioMuta; PRPS2; -.
DR DMDM; 125583; -.
DR REPRODUCTION-2DPAGE; IPI00219617; -.
DR REPRODUCTION-2DPAGE; P11908; -.
DR EPD; P11908; -.
DR jPOST; P11908; -.
DR MassIVE; P11908; -.
DR MaxQB; P11908; -.
DR PaxDb; P11908; -.
DR PeptideAtlas; P11908; -.
DR PRIDE; P11908; -.
DR ProteomicsDB; 52809; -. [P11908-1]
DR ProteomicsDB; 52810; -. [P11908-2]
DR Antibodypedia; 8471; 248 antibodies from 29 providers.
DR DNASU; 5634; -.
DR Ensembl; ENST00000380668.10; ENSP00000370043.5; ENSG00000101911.13. [P11908-1]
DR Ensembl; ENST00000398491.6; ENSP00000381504.2; ENSG00000101911.13. [P11908-2]
DR GeneID; 5634; -.
DR KEGG; hsa:5634; -.
DR MANE-Select; ENST00000380668.10; ENSP00000370043.5; NM_002765.5; NP_002756.1.
DR UCSC; uc004cva.4; human. [P11908-1]
DR CTD; 5634; -.
DR DisGeNET; 5634; -.
DR GeneCards; PRPS2; -.
DR HGNC; HGNC:9465; PRPS2.
DR HPA; ENSG00000101911; Tissue enhanced (ovary, parathyroid gland).
DR MIM; 311860; gene.
DR neXtProt; NX_P11908; -.
DR OpenTargets; ENSG00000101911; -.
DR PharmGKB; PA33820; -.
DR VEuPathDB; HostDB:ENSG00000101911; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; P11908; -.
DR OMA; WSRAPIS; -.
DR PhylomeDB; P11908; -.
DR TreeFam; TF106366; -.
DR BioCyc; MetaCyc:HS02317-MON; -.
DR PathwayCommons; P11908; -.
DR Reactome; R-HSA-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR SignaLink; P11908; -.
DR SIGNOR; P11908; -.
DR UniPathway; UPA00087; UER00172.
DR BioGRID-ORCS; 5634; 20 hits in 703 CRISPR screens.
DR ChiTaRS; PRPS2; human.
DR GenomeRNAi; 5634; -.
DR Pharos; P11908; Tbio.
DR PRO; PR:P11908; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P11908; protein.
DR Bgee; ENSG00000101911; Expressed in seminal vesicle and 199 other tissues.
DR ExpressionAtlas; P11908; baseline and differential.
DR Genevisible; P11908; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0016208; F:AMP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006167; P:AMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..318
FT /note="Ribose-phosphate pyrophosphokinase 2"
FT /id="PRO_0000141074"
FT REGION 212..227
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 96..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT VAR_SEQ 102
FT /note="K -> KVGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027769"
SQ SEQUENCE 318 AA; 34769 MW; 72A2873408250C31 CRC64;
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC
GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIA EWKNCIIVSP DAGGAKRVTS
IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCTKIQVI DISMILAEAI
RRTHNGESVS YLFSHVPL
