Full text data of PRPS2
PRPS2
[Confidence: low (only semi-automatic identification from reviews)]
Ribose-phosphate pyrophosphokinase 2; 2.7.6.1 (PPRibP; Phosphoribosyl pyrophosphate synthase II; PRS-II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribose-phosphate pyrophosphokinase 2; 2.7.6.1 (PPRibP; Phosphoribosyl pyrophosphate synthase II; PRS-II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P11908
ID PRPS2_HUMAN Reviewed; 318 AA.
AC P11908; Q0VDH9; Q0VDI0; Q15245; Q2TAK7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 151.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
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
RT project: 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
RT PRPS2 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, LACK OF N-TERMINAL
RP ACETYLATION, AND MASS 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.,
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate
CC (PRPP) that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME 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-
CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed
CC of 3 homodimers (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30019.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S02778; KIHUR2.
DR RefSeq; NP_001034180.1; NM_001039091.2.
DR RefSeq; NP_002756.1; NM_002765.4.
DR UniGene; Hs.654581; -.
DR ProteinModelPortal; P11908; -.
DR SMR; P11908; 3-317.
DR IntAct; P11908; 1.
DR MINT; MINT-5000929; -.
DR STRING; 9606.ENSP00000381504; -.
DR PhosphoSite; P11908; -.
DR DMDM; 125583; -.
DR REPRODUCTION-2DPAGE; IPI00219617; -.
DR REPRODUCTION-2DPAGE; P11908; -.
DR PaxDb; P11908; -.
DR PRIDE; P11908; -.
DR DNASU; 5634; -.
DR Ensembl; ENST00000380668; ENSP00000370043; ENSG00000101911.
DR Ensembl; ENST00000398491; ENSP00000381504; ENSG00000101911.
DR GeneID; 5634; -.
DR KEGG; hsa:5634; -.
DR UCSC; uc004cvb.3; human.
DR CTD; 5634; -.
DR GeneCards; GC0XP012719; -.
DR HGNC; HGNC:9465; PRPS2.
DR MIM; 311860; gene.
DR neXtProt; NX_P11908; -.
DR PharmGKB; PA33820; -.
DR eggNOG; COG0462; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR KO; K00948; -.
DR OMA; RENITEW; -.
DR PhylomeDB; P11908; -.
DR BioCyc; MetaCyc:HS02317-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00087; UER00172.
DR GenomeRNAi; 5634; -.
DR NextBio; 21892; -.
DR PRO; PR:P11908; -.
DR ArrayExpress; P11908; -.
DR Bgee; P11908; -.
DR CleanEx; HS_PRPS2; -.
DR Genevestigator; P11908; -.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl.
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: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; IEA:UniProtKB-UniPathway.
DR GO; GO:0006167; P:AMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Complete proteome;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ribose-phosphate pyrophosphokinase 2.
FT /FTId=PRO_0000141074.
FT NP_BIND 96 101 ATP (By similarity).
FT REGION 212 227 Binding of phosphoribosylpyrophosphate
FT (Potential).
FT METAL 128 128 Magnesium (Potential).
FT METAL 130 130 Magnesium (Potential).
FT METAL 139 139 Magnesium (Potential).
FT METAL 143 143 Magnesium (Potential).
FT BINDING 130 130 ATP (By similarity).
FT SITE 2 2 Not acetylated.
FT VAR_SEQ 102 102 K -> KVGE (in isoform 2).
FT /FTId=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
//
ID PRPS2_HUMAN Reviewed; 318 AA.
AC P11908; Q0VDH9; Q0VDI0; Q15245; Q2TAK7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 151.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
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
RT project: 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
RT PRPS2 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, LACK OF N-TERMINAL
RP ACETYLATION, AND MASS 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.,
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate
CC (PRPP) that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME 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-
CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed
CC of 3 homodimers (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30019.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S02778; KIHUR2.
DR RefSeq; NP_001034180.1; NM_001039091.2.
DR RefSeq; NP_002756.1; NM_002765.4.
DR UniGene; Hs.654581; -.
DR ProteinModelPortal; P11908; -.
DR SMR; P11908; 3-317.
DR IntAct; P11908; 1.
DR MINT; MINT-5000929; -.
DR STRING; 9606.ENSP00000381504; -.
DR PhosphoSite; P11908; -.
DR DMDM; 125583; -.
DR REPRODUCTION-2DPAGE; IPI00219617; -.
DR REPRODUCTION-2DPAGE; P11908; -.
DR PaxDb; P11908; -.
DR PRIDE; P11908; -.
DR DNASU; 5634; -.
DR Ensembl; ENST00000380668; ENSP00000370043; ENSG00000101911.
DR Ensembl; ENST00000398491; ENSP00000381504; ENSG00000101911.
DR GeneID; 5634; -.
DR KEGG; hsa:5634; -.
DR UCSC; uc004cvb.3; human.
DR CTD; 5634; -.
DR GeneCards; GC0XP012719; -.
DR HGNC; HGNC:9465; PRPS2.
DR MIM; 311860; gene.
DR neXtProt; NX_P11908; -.
DR PharmGKB; PA33820; -.
DR eggNOG; COG0462; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR KO; K00948; -.
DR OMA; RENITEW; -.
DR PhylomeDB; P11908; -.
DR BioCyc; MetaCyc:HS02317-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00087; UER00172.
DR GenomeRNAi; 5634; -.
DR NextBio; 21892; -.
DR PRO; PR:P11908; -.
DR ArrayExpress; P11908; -.
DR Bgee; P11908; -.
DR CleanEx; HS_PRPS2; -.
DR Genevestigator; P11908; -.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl.
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: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; IEA:UniProtKB-UniPathway.
DR GO; GO:0006167; P:AMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Complete proteome;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ribose-phosphate pyrophosphokinase 2.
FT /FTId=PRO_0000141074.
FT NP_BIND 96 101 ATP (By similarity).
FT REGION 212 227 Binding of phosphoribosylpyrophosphate
FT (Potential).
FT METAL 128 128 Magnesium (Potential).
FT METAL 130 130 Magnesium (Potential).
FT METAL 139 139 Magnesium (Potential).
FT METAL 143 143 Magnesium (Potential).
FT BINDING 130 130 ATP (By similarity).
FT SITE 2 2 Not acetylated.
FT VAR_SEQ 102 102 K -> KVGE (in isoform 2).
FT /FTId=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
//
MIM
311860
*RECORD*
*FIELD* NO
311860
*FIELD* TI
*311860 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE II; PRPS2
*FIELD* TX
CLONING
Five-phosphoribosyl 1-pyrophosphate (PPRibP), an essential substrate and
read morea critical regulator in the purine, pyrimidine, and pyridine nucleotide
production pathways, is synthesized from MgATP and ribose 5-phosphate by
the enzyme PPRibP synthetase (EC 2.7.6.1). By cDNA cloning, Taira et al.
(1987) found 2 distinct PPRibP synthetase subunits, PRS I (PRPS1;
311850) and PRS II. By screening a testis library with a rat PRS II
cDNA, Iizasa et al. (1989) isolated cDNAs encoding human PRS II. The
predicted 318-amino acid protein shares 99% identity with rat PRS II.
Northern blot analysis revealed that PRS II is expressed as a 2.7-kb
mRNA in testis.
By Northern blot analysis using rat Prps2 as probe, Taira et al. (1989)
detected a 2.7-kb transcript in human testis and in 2 human cell lines.
GENE FUNCTION
Wang et al. (1992) demonstrated that the PRPS2 gene is inactivated with
lyonization but that it lies between 2 genes that escape inactivation,
STS (300747) distally and ZFX (314980) proximally. The PRPS1 gene also
undergoes X inactivation. Wang et al. (1992) commented that it was not
known which of the 2 PRPS loci is altered in patients with inherited
PRPS superactivity. The ZFX gene, which escapes X-inactivation, is
bracketed proximally by the POLA gene (312040) which, like PRPS2,
undergoes inactivation. The A1S9T (314370) locus in the proximal short
arm and the RPS4X gene (312760) in the proximal long arm are other loci
that escape inactivation and are interspersed among genes that do
undergo X-inactivation. Furthermore, the XIST gene (314670), located at
Xq13, is transcribed only from the inactive X chromosome.
MAPPING
By using a rat cDNA probe for PRPS1 and a human cDNA probe for PRPS2,
Taira et al. (1989) showed in DNA from somatic cell hybrids and in
spot-blot hybridization of flow-sorted chromosomes that whereas PRPS1 is
on Xq21-qter, PRPS2 is on Xpter-q21. Furthermore, 2 PRPS1-related genes
were identified on chromosomes 7 and 9. By a combination of in situ
hybridization and study of human/rodent somatic cell hybrids, Becker et
al. (1990) assigned the PRPS2 locus to Xp22.3-p22.2. Despite the
striking homology in the cDNA sequence and deduced amino acid sequence,
PRPS1 and PRPS2 are encoded by genes on opposite arms of the X
chromosome.
*FIELD* RF
1. Becker, M. A.; Heidler, S. A.; Bell, G. I.; Seino, S.; Le Beau,
M. M.; Westbrook, C. A.; Neuman, W.; Shapiro, L. J.; Mohandas, T.
K.; Roessler, B. J.; Palella, T. D.: Cloning of cDNAs for human phosphoribosylpyrophosphate
synthetases 1 and 2 and X chromosome localization of PRPS1 and PRPS2
genes. Genomics 8: 555-561, 1990.
2. Iizasa, T.; Taira, M.; Shimada, H.; Ishijima, S.; Tatibana, M.
: Molecular cloning and sequencing of human cDNA for phosphoribosyl
pyrophosphate synthetase subunit II. FEBS Lett. 244: 47-50, 1989.
3. Taira, M.; Iizasa, T.; Yamada, K.; Shimada, H.; Tatibana, M.:
Tissue-differential expression of two distinct genes for phosphoribosyl
pyrophosphate synthetase and existence of the testis-specific transcript. Biochim.
Biophys. Acta 1007: 203-208, 1989.
4. Taira, M.; Ishijima, S.; Kita, K.; Yamada, K.; Iizasa, T.; Tatibana,
M.: Nucleotide and deduced amino acid sequences of two distinct cDNAs
for rat phosphoribosylpyrophosphate synthetase. J. Biol. Chem. 262:
14867-14870, 1987.
5. Taira, M.; Kudoh, J.; Minoshima, S.; Iizasa, T.; Shimada, H.; Shimizu,
Y.; Tatibana, M.; Shimizu, N.: Localization of human phosphoribosylpyrophosphate
synthetase subunit I and II genes (PRPS1 and PRPS2) to different regions
of the X chromosome and assignment of two PRPS1-related genes to autosomes. Somat.
Cell Molec. Genet. 15: 29-37, 1989.
6. Wang, J. C.; Passage, M. B.; Ellison, J.; Becker, M. A.; Yen, P.
H.; Shapiro, L. J.; Mohandas, T. K.: Physical mapping of loci in
the distal half of the short arm of the human X chromosome: implications
for the spreading of X-chromosome inactivation. Somat. Cell Molec.
Genet. 18: 195-200, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/24/2007
Rebekah S. Rasooly - updated: 2/24/1999
*FIELD* CD
Victor A. McKusick: 3/14/1989
*FIELD* ED
carol: 10/31/2008
mgross: 10/30/2007
terry: 10/24/2007
alopez: 2/24/1999
dkim: 7/7/1998
mimadm: 2/28/1994
carol: 8/13/1992
supermim: 3/17/1992
carol: 12/11/1990
supermim: 3/20/1990
ddp: 10/26/1989
*RECORD*
*FIELD* NO
311860
*FIELD* TI
*311860 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE II; PRPS2
*FIELD* TX
CLONING
Five-phosphoribosyl 1-pyrophosphate (PPRibP), an essential substrate and
read morea critical regulator in the purine, pyrimidine, and pyridine nucleotide
production pathways, is synthesized from MgATP and ribose 5-phosphate by
the enzyme PPRibP synthetase (EC 2.7.6.1). By cDNA cloning, Taira et al.
(1987) found 2 distinct PPRibP synthetase subunits, PRS I (PRPS1;
311850) and PRS II. By screening a testis library with a rat PRS II
cDNA, Iizasa et al. (1989) isolated cDNAs encoding human PRS II. The
predicted 318-amino acid protein shares 99% identity with rat PRS II.
Northern blot analysis revealed that PRS II is expressed as a 2.7-kb
mRNA in testis.
By Northern blot analysis using rat Prps2 as probe, Taira et al. (1989)
detected a 2.7-kb transcript in human testis and in 2 human cell lines.
GENE FUNCTION
Wang et al. (1992) demonstrated that the PRPS2 gene is inactivated with
lyonization but that it lies between 2 genes that escape inactivation,
STS (300747) distally and ZFX (314980) proximally. The PRPS1 gene also
undergoes X inactivation. Wang et al. (1992) commented that it was not
known which of the 2 PRPS loci is altered in patients with inherited
PRPS superactivity. The ZFX gene, which escapes X-inactivation, is
bracketed proximally by the POLA gene (312040) which, like PRPS2,
undergoes inactivation. The A1S9T (314370) locus in the proximal short
arm and the RPS4X gene (312760) in the proximal long arm are other loci
that escape inactivation and are interspersed among genes that do
undergo X-inactivation. Furthermore, the XIST gene (314670), located at
Xq13, is transcribed only from the inactive X chromosome.
MAPPING
By using a rat cDNA probe for PRPS1 and a human cDNA probe for PRPS2,
Taira et al. (1989) showed in DNA from somatic cell hybrids and in
spot-blot hybridization of flow-sorted chromosomes that whereas PRPS1 is
on Xq21-qter, PRPS2 is on Xpter-q21. Furthermore, 2 PRPS1-related genes
were identified on chromosomes 7 and 9. By a combination of in situ
hybridization and study of human/rodent somatic cell hybrids, Becker et
al. (1990) assigned the PRPS2 locus to Xp22.3-p22.2. Despite the
striking homology in the cDNA sequence and deduced amino acid sequence,
PRPS1 and PRPS2 are encoded by genes on opposite arms of the X
chromosome.
*FIELD* RF
1. Becker, M. A.; Heidler, S. A.; Bell, G. I.; Seino, S.; Le Beau,
M. M.; Westbrook, C. A.; Neuman, W.; Shapiro, L. J.; Mohandas, T.
K.; Roessler, B. J.; Palella, T. D.: Cloning of cDNAs for human phosphoribosylpyrophosphate
synthetases 1 and 2 and X chromosome localization of PRPS1 and PRPS2
genes. Genomics 8: 555-561, 1990.
2. Iizasa, T.; Taira, M.; Shimada, H.; Ishijima, S.; Tatibana, M.
: Molecular cloning and sequencing of human cDNA for phosphoribosyl
pyrophosphate synthetase subunit II. FEBS Lett. 244: 47-50, 1989.
3. Taira, M.; Iizasa, T.; Yamada, K.; Shimada, H.; Tatibana, M.:
Tissue-differential expression of two distinct genes for phosphoribosyl
pyrophosphate synthetase and existence of the testis-specific transcript. Biochim.
Biophys. Acta 1007: 203-208, 1989.
4. Taira, M.; Ishijima, S.; Kita, K.; Yamada, K.; Iizasa, T.; Tatibana,
M.: Nucleotide and deduced amino acid sequences of two distinct cDNAs
for rat phosphoribosylpyrophosphate synthetase. J. Biol. Chem. 262:
14867-14870, 1987.
5. Taira, M.; Kudoh, J.; Minoshima, S.; Iizasa, T.; Shimada, H.; Shimizu,
Y.; Tatibana, M.; Shimizu, N.: Localization of human phosphoribosylpyrophosphate
synthetase subunit I and II genes (PRPS1 and PRPS2) to different regions
of the X chromosome and assignment of two PRPS1-related genes to autosomes. Somat.
Cell Molec. Genet. 15: 29-37, 1989.
6. Wang, J. C.; Passage, M. B.; Ellison, J.; Becker, M. A.; Yen, P.
H.; Shapiro, L. J.; Mohandas, T. K.: Physical mapping of loci in
the distal half of the short arm of the human X chromosome: implications
for the spreading of X-chromosome inactivation. Somat. Cell Molec.
Genet. 18: 195-200, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/24/2007
Rebekah S. Rasooly - updated: 2/24/1999
*FIELD* CD
Victor A. McKusick: 3/14/1989
*FIELD* ED
carol: 10/31/2008
mgross: 10/30/2007
terry: 10/24/2007
alopez: 2/24/1999
dkim: 7/7/1998
mimadm: 2/28/1994
carol: 8/13/1992
supermim: 3/17/1992
carol: 12/11/1990
supermim: 3/20/1990
ddp: 10/26/1989