ID HPRT_MOUSE Reviewed; 218 AA. AC P00493; Q545Y2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 192. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492}; DE AltName: Full=HPRT B; GN Name=Hprt1; Synonyms=Hprt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6294614; DOI=10.1093/nar/10.21.6763; RA Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C.; RT "Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese RT hamster: construction and sequence analysis of cDNA recombinants."; RL Nucleic Acids Res. 10:6763-6775(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/cJ; TISSUE=Myeloma; RX PubMed=6326107; DOI=10.1073/pnas.81.7.2147; RA Melton D.W., Konecki D.S., Brennand J., Caskey C.T.; RT "Structure, expression, and mutation of the hypoxanthine RT phosphoribosyltransferase gene."; RL Proc. Natl. Acad. Sci. U.S.A. 81:2147-2151(1984). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; 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 [5] RP PROTEIN SEQUENCE OF 74-83 AND 171-200, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine CC to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5- CC phosphoribosylpyrophosphate onto the purine. Plays a central role in CC the generation of purine nucleotides through the purine salvage pathway CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. The magnesium ions are CC essentially bound to the substrate and have few direct interactions CC with the protein. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from hypoxanthine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. {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; J00423; AAA96232.1; -; mRNA. DR EMBL; K01515; AAA96271.1; -; Genomic_DNA. DR EMBL; K01507; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01508; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01509; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01510; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01511; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01512; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01513; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; K01514; AAA96271.1; JOINED; Genomic_DNA. DR EMBL; AK002286; BAB21989.1; -; mRNA. DR EMBL; AK088114; BAC40153.1; -; mRNA. DR EMBL; AK146626; BAE27315.1; -; mRNA. DR EMBL; BC083145; AAH83145.1; -; mRNA. DR CCDS; CCDS40972.1; -. DR PIR; I49756; RTMSG. DR RefSeq; NP_038584.2; NM_013556.2. DR AlphaFoldDB; P00493; -. DR SMR; P00493; -. DR BioGRID; 200411; 16. DR DIP; DIP-6034N; -. DR MINT; P00493; -. DR STRING; 10090.ENSMUSP00000026723; -. DR ChEMBL; CHEMBL3243916; -. DR GlyGen; P00493; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P00493; -. DR MetOSite; P00493; -. DR PhosphoSitePlus; P00493; -. DR SwissPalm; P00493; -. DR EPD; P00493; -. DR jPOST; P00493; -. DR MaxQB; P00493; -. DR PaxDb; 10090-ENSMUSP00000026723; -. DR PeptideAtlas; P00493; -. DR ProteomicsDB; 267060; -. DR Pumba; P00493; -. DR Antibodypedia; 1912; 685 antibodies from 37 providers. DR DNASU; 15452; -. DR Ensembl; ENSMUST00000026723.9; ENSMUSP00000026723.9; ENSMUSG00000025630.9. DR GeneID; 15452; -. DR KEGG; mmu:15452; -. DR UCSC; uc009ter.1; mouse. DR AGR; MGI:96217; -. DR CTD; 3251; -. DR MGI; MGI:96217; Hprt1. DR VEuPathDB; HostDB:ENSMUSG00000025630; -. DR eggNOG; KOG3367; Eukaryota. DR GeneTree; ENSGT00940000155028; -. DR HOGENOM; CLU_073615_3_0_1; -. DR InParanoid; P00493; -. DR OMA; MQWRVAP; -. DR OrthoDB; 4216383at2759; -. DR PhylomeDB; P00493; -. DR TreeFam; TF313367; -. DR Reactome; R-MMU-74217; Purine salvage. DR Reactome; R-MMU-9748787; Azathioprine ADME. DR UniPathway; UPA00591; UER00648. DR BioGRID-ORCS; 15452; 1 hit in 79 CRISPR screens. DR ChiTaRS; Hprt; mouse. DR PRO; PR:P00493; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; P00493; Protein. DR Bgee; ENSMUSG00000025630; Expressed in cleaving embryo and 289 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IMP:MGI. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0046083; P:adenine metabolic process; IGI:MGI. DR GO; GO:0044209; P:AMP salvage; IDA:MGI. DR GO; GO:0021954; P:central nervous system neuron development; IMP:MGI. DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI. DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI. DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI. DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI. DR GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB. DR GO; GO:0032263; P:GMP salvage; IMP:MGI. DR GO; GO:0007625; P:grooming behavior; IGI:MGI. DR GO; GO:0006178; P:guanine salvage; ISO:MGI. DR GO; GO:0046100; P:hypoxanthine metabolic process; IMP:MGI. DR GO; GO:0043103; P:hypoxanthine salvage; ISS:UniProtKB. DR GO; GO:0046040; P:IMP metabolic process; ISS:UniProtKB. DR GO; GO:0032264; P:IMP salvage; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:MGI. DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; ISO:MGI. DR GO; GO:0006166; P:purine ribonucleoside salvage; IMP:MGI. DR GO; GO:0001975; P:response to amphetamine; IMP:MGI. DR GO; GO:0021756; P:striatum development; IMP:MGI. DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR005904; Hxn_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR NCBIfam; TIGR01203; HGPRTase; 1. DR PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43340:SF6; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. DR Genevisible; P00493; MM. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Glycosyltransferase; KW Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Purine salvage; Reference proteome; Transferase; KW Ubl conjugation. FT CHAIN 1..218 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139588" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 134..142 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 166 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 186..188 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 103 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 142 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P27605" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P00492" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P00492" FT CONFLICT 201 FT /note="D -> N (in Ref. 1; AAA96232)" FT /evidence="ECO:0000305" SQ SEQUENCE 218 AA; 24570 MW; 925CC0D4A6626E05 CRC64; MPTRSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA //