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P00492

- HPRT_HUMAN

UniProt

P00492 - HPRT_HUMAN

Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

HPRT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.

    Catalytic activityi

    IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
    GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.

    Cofactori

    Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.

    Kineticsi

    1. KM=5.4 µM for IMP1 Publication
    2. KM=0.45 µM for hypoxanthine1 Publication
    3. KM=25 µM for pyrophosphate1 Publication
    4. KM=31 µM for phosphoribosylpyrophosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691GMP1 Publication
    Active sitei138 – 1381Proton acceptorCurated
    Binding sitei166 – 1661GMP1 Publication
    Metal bindingi194 – 1941Magnesium
    Binding sitei194 – 1941GMP; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi134 – 1429GMP1 Publication
    Nucleotide bindingi186 – 1883GMP1 Publication

    GO - Molecular functioni

    1. guanine phosphoribosyltransferase activity Source: UniProtKB
    2. hypoxanthine phosphoribosyltransferase activity Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB
    4. nucleotide binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. adenine salvage Source: RefGenome
    2. central nervous system neuron development Source: Ensembl
    3. cerebral cortex neuron differentiation Source: Ensembl
    4. cytolysis Source: Ensembl
    5. dendrite morphogenesis Source: Ensembl
    6. dopamine metabolic process Source: Ensembl
    7. GMP catabolic process Source: UniProtKB
    8. GMP salvage Source: RefGenome
    9. grooming behavior Source: Ensembl
    10. guanine salvage Source: UniProtKB
    11. hypoxanthine metabolic process Source: UniProtKB
    12. hypoxanthine salvage Source: UniProtKB
    13. IMP metabolic process Source: UniProtKB
    14. IMP salvage Source: RefGenome
    15. locomotory behavior Source: Ensembl
    16. lymphocyte proliferation Source: Ensembl
    17. nucleobase-containing small molecule metabolic process Source: Reactome
    18. positive regulation of dopamine metabolic process Source: UniProtKB
    19. protein homotetramerization Source: UniProtKB
    20. purine-containing compound salvage Source: Reactome
    21. purine nucleobase metabolic process Source: Reactome
    22. purine nucleotide biosynthetic process Source: UniProtKB
    23. purine ribonucleoside salvage Source: UniProtKB
    24. response to amphetamine Source: Ensembl
    25. small molecule metabolic process Source: Reactome
    26. striatum development Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09275-MONOMER.
    ReactomeiREACT_1923. Purine salvage.
    SABIO-RKP00492.
    UniPathwayiUPA00591; UER00648.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
    Short name:
    HGPRT
    Short name:
    HGPRTase
    Gene namesi
    Name:HPRT1
    Synonyms:HPRT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:5157. HPRT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Lesch-Nyhan syndrome (LNS) [MIM:300322]: Characterized by complete lack of enzymatic activity that results in hyperuricemia, choreoathetosis, mental retardation, and compulsive self-mutilation.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81V → G in LNS; HB.
    VAR_006751
    Natural varianti16 – 161G → D in LNS; FG.
    VAR_006752
    Natural varianti28 – 281Missing in LNS. 1 Publication
    VAR_012312
    Natural varianti41 – 411L → P in LNS; Detroit.
    VAR_006756
    Natural varianti42 – 421I → F in LNS; Isar. 1 Publication
    VAR_006757
    Natural varianti42 – 421I → T in LNS; Heapey.
    VAR_006758
    Natural varianti43 – 442MD → RN in LNS; Salamanca.
    VAR_006759
    Natural varianti45 – 451R → K in LNS; RJK 2163. 1 Publication
    VAR_006760
    Natural varianti50 – 501A → P in LNS; LW.
    VAR_006763
    Natural varianti50 – 501A → V in LNS; 1265. 1 Publication
    VAR_006762
    Natural varianti51 – 511R → P in LNS; Banbury.
    VAR_006765
    Natural varianti54 – 541M → L in LNS; Japan-1.
    VAR_006769
    Natural varianti57 – 571M → T in LNS; Montreal. 1 Publication
    VAR_006770
    Natural varianti70 – 701G → E in LNS; New Haven/1510. 1 Publication
    VAR_006773
    Natural varianti71 – 711G → R in LNS; Yale. 1 Publication
    VAR_006774
    Natural varianti74 – 741F → L in LNS; Flint/RJK 892/DW/Perth/1522. 3 Publications
    VAR_006775
    Natural varianti130 – 1301V → D in LNS; Midland/RJK 896. 2 Publications
    VAR_006780
    Natural varianti131 – 1311L → S in LNS; RJK 1784. 1 Publication
    VAR_006781
    Natural varianti132 – 1321I → T in LNS; Runcorn.
    VAR_006783
    Natural varianti143 – 1431M → K in LNS; RJK 1210. 1 Publication
    VAR_006785
    Natural varianti143 – 1431M → MA in LNS; RW.
    VAR_006786
    Natural varianti162 – 1621S → R in LNS; Farnham.
    VAR_006788
    Natural varianti176 – 1761P → L in LNS; Marlow.
    VAR_006790
    Natural varianti177 – 1771D → V in LNS; Roanne. 1 Publication
    VAR_006791
    Natural varianti177 – 1771D → Y in LNS; RJK 2185. 1 Publication
    VAR_006792
    Natural varianti179 – 1791Missing in LNS; Michigan.
    VAR_006793
    Natural varianti194 – 1941D → N in LNS; Kinston/RJK 2188. 2 Publications
    VAR_006798
    Natural varianti199 – 1991F → V in LNS; New Briton/RJK 950. 1 Publication
    VAR_006800
    Natural varianti201 – 2011D → Y in LNS; GM.
    VAR_006803
    Natural varianti204 – 2041H → D in LNS; RJK 1874. 1 Publication
    VAR_006804
    Natural varianti204 – 2041H → R in LNS; 779. 1 Publication
    VAR_006805
    Natural varianti206 – 2061C → Y in LNS; Reading/RJK 1727. 1 Publication
    VAR_006806
    Gout HPRT-related (GOUT-HPRT) [MIM:300323]: Characterized by partial enzyme activity and hyperuricemia.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71G → D in GOUT-HPRT; Gravesend.
    VAR_006750
    Natural varianti16 – 161G → S in GOUT-HPRT; Urangan.
    VAR_006753
    Natural varianti20 – 201D → V in GOUT-HPRT; Mashad.
    VAR_006754
    Natural varianti23 – 231C → W in GOUT-HPRT; JS.
    VAR_006755
    Natural varianti48 – 481R → H in GOUT-HPRT; AD and DD.
    VAR_006761
    Natural varianti51 – 511R → G in GOUT-HPRT; Toronto. 1 Publication
    VAR_006764
    Natural varianti53 – 531V → A in GOUT-HPRT; MG.
    VAR_006767
    Natural varianti53 – 531V → M in GOUT-HPRT; TE.
    VAR_006768
    Natural varianti58 – 581G → R in GOUT-HPRT; Toowong.
    VAR_006771
    Natural varianti78 – 781L → V in GOUT-HPRT; Swan.
    VAR_006776
    Natural varianti80 – 801D → V in GOUT-HPRT; Arlington.
    VAR_006777
    Natural varianti104 – 1041S → R in GOUT-HPRT; Munich. 2 Publications
    VAR_006778
    Natural varianti110 – 1101S → L in GOUT-HPRT; London. 2 Publications
    VAR_006779
    Natural varianti132 – 1321I → M in GOUT-HPRT; Ann-Arbor.
    VAR_006782
    Natural varianti135 – 1351D → G in GOUT-HPRT; Yeronga.
    VAR_006784
    Natural varianti161 – 1611A → S in GOUT-HPRT; Milwaukee/RJK 949. 1 Publication
    VAR_006787
    Natural varianti168 – 1681T → I in GOUT-HPRT; Brisbane. 1 Publication
    VAR_006789
    Natural varianti179 – 1802VG → GR in GOUT-HPRT; Japan-2.
    VAR_006794
    Natural varianti183 – 1831I → T in GOUT-HPRT; JF. 1 Publication
    VAR_006796
    Natural varianti194 – 1941D → E in GOUT-HPRT; Moose-Jaw; results in cooperativity and decreased substrate affinities. 1 Publication
    VAR_006797
    Natural varianti195 – 1951Y → C in GOUT-HPRT; Dirranbandi.
    VAR_006799
    Natural varianti201 – 2011D → G in GOUT-HPRT; Ashville. 1 Publication
    VAR_006801
    Natural varianti201 – 2011D → N in GOUT-HPRT; RB.
    VAR_006802

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691K → A: Reduced affinity for hypoxanthine, phosphoribosylpyrophosphate and IMP. Reduced catalytic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Gout

    Organism-specific databases

    MIMi300322. phenotype.
    300323. phenotype.
    Orphaneti79233. Hypoxanthine guanine phosphoribosyltransferase partial deficiency.
    510. Lesch-Nyhan syndrome.
    PharmGKBiPA29427.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 218217Hypoxanthine-guanine phosphoribosyltransferasePRO_0000139585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei103 – 1031N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP00492.
    PaxDbiP00492.
    PeptideAtlasiP00492.
    PRIDEiP00492.

    2D gel databases

    OGPiP00492.
    REPRODUCTION-2DPAGEIPI00218493.

    PTM databases

    PhosphoSiteiP00492.

    Expressioni

    Gene expression databases

    BgeeiP00492.
    CleanExiHS_HPRT1.
    GenevestigatoriP00492.

    Organism-specific databases

    HPAiCAB012200.
    HPA006360.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WDYHV1Q96HA83EBI-748210,EBI-741158

    Protein-protein interaction databases

    BioGridi109488. 23 interactions.
    IntActiP00492. 4 interactions.
    MINTiMINT-1443310.
    STRINGi9606.ENSP00000298556.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Beta strandi12 – 143
    Helixi19 – 213
    Helixi26 – 283
    Turni29 – 313
    Beta strandi32 – 376
    Helixi39 – 5719
    Beta strandi62 – 676
    Turni69 – 713
    Helixi73 – 8614
    Beta strandi88 – 903
    Beta strandi95 – 1006
    Beta strandi109 – 11810
    Helixi122 – 1254
    Beta strandi128 – 1369
    Helixi140 – 15112
    Beta strandi156 – 16611
    Beta strandi177 – 1837
    Beta strandi188 – 1903
    Beta strandi195 – 1973
    Beta strandi198 – 2014
    Beta strandi204 – 2085
    Helixi210 – 2167

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BZYX-ray2.00A/B/C/D2-218[»]
    1D6NX-ray2.70A/B5-218[»]
    1HMPX-ray2.50A/B2-218[»]
    1Z7GX-ray1.90A/B/C/D2-218[»]
    2VFAX-ray2.80A/B49-160[»]
    3GEPX-ray2.60A/B2-218[»]
    3GGCX-ray2.78A/B2-218[»]
    3GGJX-ray2.60A/B2-218[»]
    4IJQX-ray2.00A/B/C/D2-218[»]
    4KN6X-ray2.73A3-218[»]
    ProteinModelPortaliP00492.
    SMRiP00492. Positions 5-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00492.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0634.
    HOGENOMiHOG000236521.
    HOVERGENiHBG000242.
    KOiK00760.
    OMAiVDFMTVS.
    OrthoDBiEOG7673CK.
    PhylomeDBiP00492.
    TreeFamiTF313367.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00492-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA    50
    RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI 100
    RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV 150
    RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR 200
    DLNHVCVISE TGKAKYKA 218
    Length:218
    Mass (Da):24,579
    Last modified:January 23, 2007 - v2
    Checksum:i1928EE69517CCB40
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71G → D in GOUT-HPRT; Gravesend.
    VAR_006750
    Natural varianti8 – 81V → G in LNS; HB.
    VAR_006751
    Natural varianti16 – 161G → D in LNS; FG.
    VAR_006752
    Natural varianti16 – 161G → S in GOUT-HPRT; Urangan.
    VAR_006753
    Natural varianti20 – 201D → V in GOUT-HPRT; Mashad.
    VAR_006754
    Natural varianti23 – 231C → W in GOUT-HPRT; JS.
    VAR_006755
    Natural varianti28 – 281Missing in LNS. 1 Publication
    VAR_012312
    Natural varianti41 – 411L → P in LNS; Detroit.
    VAR_006756
    Natural varianti42 – 421I → F in LNS; Isar. 1 Publication
    VAR_006757
    Natural varianti42 – 421I → T in LNS; Heapey.
    VAR_006758
    Natural varianti43 – 442MD → RN in LNS; Salamanca.
    VAR_006759
    Natural varianti45 – 451R → K in LNS; RJK 2163. 1 Publication
    VAR_006760
    Natural varianti48 – 481R → H in GOUT-HPRT; AD and DD.
    VAR_006761
    Natural varianti50 – 501A → P in LNS; LW.
    VAR_006763
    Natural varianti50 – 501A → V in LNS; 1265. 1 Publication
    VAR_006762
    Natural varianti51 – 511R → G in GOUT-HPRT; Toronto. 1 Publication
    VAR_006764
    Natural varianti51 – 511R → P in LNS; Banbury.
    VAR_006765
    Natural varianti52 – 521D → G in Edinburgh. 1 Publication
    VAR_006766
    Natural varianti53 – 531V → A in GOUT-HPRT; MG.
    VAR_006767
    Natural varianti53 – 531V → M in GOUT-HPRT; TE.
    VAR_006768
    Natural varianti54 – 541M → L in LNS; Japan-1.
    VAR_006769
    Natural varianti57 – 571M → T in LNS; Montreal. 1 Publication
    VAR_006770
    Natural varianti58 – 581G → R in GOUT-HPRT; Toowong.
    VAR_006771
    Natural varianti61 – 611H → R Enzyme activity 37% of normal; asymptomatic. 1 Publication
    VAR_006772
    Natural varianti70 – 701G → E in LNS; New Haven/1510. 1 Publication
    VAR_006773
    Natural varianti71 – 711G → R in LNS; Yale. 1 Publication
    VAR_006774
    Natural varianti74 – 741F → L in LNS; Flint/RJK 892/DW/Perth/1522. 3 Publications
    VAR_006775
    Natural varianti78 – 781L → V in GOUT-HPRT; Swan.
    VAR_006776
    Natural varianti80 – 801D → V in GOUT-HPRT; Arlington.
    VAR_006777
    Natural varianti104 – 1041S → R in GOUT-HPRT; Munich. 2 Publications
    VAR_006778
    Natural varianti110 – 1101S → L in GOUT-HPRT; London. 2 Publications
    VAR_006779
    Natural varianti130 – 1301V → D in LNS; Midland/RJK 896. 2 Publications
    VAR_006780
    Natural varianti131 – 1311L → S in LNS; RJK 1784. 1 Publication
    VAR_006781
    Natural varianti132 – 1321I → M in GOUT-HPRT; Ann-Arbor.
    VAR_006782
    Natural varianti132 – 1321I → T in LNS; Runcorn.
    VAR_006783
    Natural varianti135 – 1351D → G in GOUT-HPRT; Yeronga.
    VAR_006784
    Natural varianti143 – 1431M → K in LNS; RJK 1210. 1 Publication
    VAR_006785
    Natural varianti143 – 1431M → MA in LNS; RW.
    VAR_006786
    Natural varianti161 – 1611A → S in GOUT-HPRT; Milwaukee/RJK 949. 1 Publication
    VAR_006787
    Natural varianti162 – 1621S → R in LNS; Farnham.
    VAR_006788
    Natural varianti168 – 1681T → I in GOUT-HPRT; Brisbane. 1 Publication
    VAR_006789
    Natural varianti176 – 1761P → L in LNS; Marlow.
    VAR_006790
    Natural varianti177 – 1771D → V in LNS; Roanne. 1 Publication
    VAR_006791
    Natural varianti177 – 1771D → Y in LNS; RJK 2185. 1 Publication
    VAR_006792
    Natural varianti179 – 1802VG → GR in GOUT-HPRT; Japan-2.
    VAR_006794
    Natural varianti179 – 1791Missing in LNS; Michigan.
    VAR_006793
    Natural varianti183 – 1831I → T in GOUT-HPRT; JF. 1 Publication
    VAR_006796
    Natural varianti188 – 1881V → A in Japan. 1 Publication
    VAR_006795
    Natural varianti194 – 1941D → E in GOUT-HPRT; Moose-Jaw; results in cooperativity and decreased substrate affinities. 1 Publication
    VAR_006797
    Natural varianti194 – 1941D → N in LNS; Kinston/RJK 2188. 2 Publications
    VAR_006798
    Natural varianti195 – 1951Y → C in GOUT-HPRT; Dirranbandi.
    VAR_006799
    Natural varianti199 – 1991F → V in LNS; New Briton/RJK 950. 1 Publication
    VAR_006800
    Natural varianti201 – 2011D → G in GOUT-HPRT; Ashville. 1 Publication
    VAR_006801
    Natural varianti201 – 2011D → N in GOUT-HPRT; RB.
    VAR_006802
    Natural varianti201 – 2011D → Y in LNS; GM.
    VAR_006803
    Natural varianti204 – 2041H → D in LNS; RJK 1874. 1 Publication
    VAR_006804
    Natural varianti204 – 2041H → R in LNS; 779. 1 Publication
    VAR_006805
    Natural varianti206 – 2061C → Y in LNS; Reading/RJK 1727. 1 Publication
    VAR_006806

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31642 mRNA. Translation: AAA52690.1.
    M26434 Genomic DNA. Translation: AAA36012.1.
    AK313435 mRNA. Translation: BAG36226.1.
    BT019350 mRNA. Translation: AAV38157.1.
    AY780550 Genomic DNA. Translation: AAV31777.1.
    AC004383 Genomic DNA. No translation available.
    CH471107 Genomic DNA. Translation: EAX11761.1.
    BC000578 mRNA. Translation: AAH00578.1.
    M12452 Genomic DNA. Translation: AAA52691.1.
    S79313 Genomic DNA. Translation: AAB21289.1.
    L29383 mRNA. Translation: AAB59391.1.
    L29382 mRNA. Translation: AAB59392.1.
    S60300 mRNA. Translation: AAC60591.2.
    CCDSiCCDS14641.1.
    PIRiA32728. RTHUG.
    RefSeqiNP_000185.1. NM_000194.2.
    UniGeneiHs.412707.

    Genome annotation databases

    EnsembliENST00000298556; ENSP00000298556; ENSG00000165704.
    GeneIDi3251.
    KEGGihsa:3251.
    UCSCiuc004exl.4. human.

    Polymorphism databases

    DMDMi123497.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Hypoxanthine-guanine phosphoribosyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31642 mRNA. Translation: AAA52690.1 .
    M26434 Genomic DNA. Translation: AAA36012.1 .
    AK313435 mRNA. Translation: BAG36226.1 .
    BT019350 mRNA. Translation: AAV38157.1 .
    AY780550 Genomic DNA. Translation: AAV31777.1 .
    AC004383 Genomic DNA. No translation available.
    CH471107 Genomic DNA. Translation: EAX11761.1 .
    BC000578 mRNA. Translation: AAH00578.1 .
    M12452 Genomic DNA. Translation: AAA52691.1 .
    S79313 Genomic DNA. Translation: AAB21289.1 .
    L29383 mRNA. Translation: AAB59391.1 .
    L29382 mRNA. Translation: AAB59392.1 .
    S60300 mRNA. Translation: AAC60591.2 .
    CCDSi CCDS14641.1.
    PIRi A32728. RTHUG.
    RefSeqi NP_000185.1. NM_000194.2.
    UniGenei Hs.412707.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BZY X-ray 2.00 A/B/C/D 2-218 [» ]
    1D6N X-ray 2.70 A/B 5-218 [» ]
    1HMP X-ray 2.50 A/B 2-218 [» ]
    1Z7G X-ray 1.90 A/B/C/D 2-218 [» ]
    2VFA X-ray 2.80 A/B 49-160 [» ]
    3GEP X-ray 2.60 A/B 2-218 [» ]
    3GGC X-ray 2.78 A/B 2-218 [» ]
    3GGJ X-ray 2.60 A/B 2-218 [» ]
    4IJQ X-ray 2.00 A/B/C/D 2-218 [» ]
    4KN6 X-ray 2.73 A 3-218 [» ]
    ProteinModelPortali P00492.
    SMRi P00492. Positions 5-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109488. 23 interactions.
    IntActi P00492. 4 interactions.
    MINTi MINT-1443310.
    STRINGi 9606.ENSP00000298556.

    Chemistry

    BindingDBi P00492.
    ChEMBLi CHEMBL2360.
    DrugBanki DB01033. Mercaptopurine.
    DB00352. Thioguanine.

    PTM databases

    PhosphoSitei P00492.

    Polymorphism databases

    DMDMi 123497.

    2D gel databases

    OGPi P00492.
    REPRODUCTION-2DPAGE IPI00218493.

    Proteomic databases

    MaxQBi P00492.
    PaxDbi P00492.
    PeptideAtlasi P00492.
    PRIDEi P00492.

    Protocols and materials databases

    DNASUi 3251.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298556 ; ENSP00000298556 ; ENSG00000165704 .
    GeneIDi 3251.
    KEGGi hsa:3251.
    UCSCi uc004exl.4. human.

    Organism-specific databases

    CTDi 3251.
    GeneCardsi GC0XP133594.
    GeneReviewsi HPRT1.
    HGNCi HGNC:5157. HPRT1.
    HPAi CAB012200.
    HPA006360.
    MIMi 300322. phenotype.
    300323. phenotype.
    308000. gene.
    neXtProti NX_P00492.
    Orphaneti 79233. Hypoxanthine guanine phosphoribosyltransferase partial deficiency.
    510. Lesch-Nyhan syndrome.
    PharmGKBi PA29427.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0634.
    HOGENOMi HOG000236521.
    HOVERGENi HBG000242.
    KOi K00760.
    OMAi VDFMTVS.
    OrthoDBi EOG7673CK.
    PhylomeDBi P00492.
    TreeFami TF313367.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00648 .
    BioCyci MetaCyc:HS09275-MONOMER.
    Reactomei REACT_1923. Purine salvage.
    SABIO-RK P00492.

    Miscellaneous databases

    ChiTaRSi HPRT1. human.
    EvolutionaryTracei P00492.
    GeneWikii Hypoxanthine-guanine_phosphoribosyltransferase.
    GenomeRNAii 3251.
    NextBioi 12927.
    PROi P00492.
    SOURCEi Search...

    Gene expression databases

    Bgeei P00492.
    CleanExi HS_HPRT1.
    Genevestigatori P00492.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    InterProi IPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01203. HGPRTase. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase."
      Jolly D.J., Okayama H., Berg P., Esty A.C., Filpula D., Bohlen P., Johnson G.G., Shively J.E., Hunkapillar T., Friedmann T.
      Proc. Natl. Acad. Sci. U.S.A. 80:477-481(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    9. "Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme."
      Wilson J.M., Tarr G.E., Mahoney W.C., Kelley W.N.
      J. Biol. Chem. 257:10978-10985(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-218, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    10. "Fine structure of the human hypoxanthine phosphoribosyltransferase gene."
      Patel P.I., Framson P.E., Caskey C.T., Chinault A.C.
      Mol. Cell. Biol. 6:393-403(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP."
      Eads J.C., Scapin G., Xu Y., Grubmeyer C., Sacchettini J.C.
      Cell 78:325-334(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GMP.
    13. "The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor."
      Shi W., Li C.M., Tyler P.C., Furneaux R.H., Grubmeyer C., Schramm V.L., Almo S.C.
      Nat. Struct. Biol. 6:588-593(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH A TRANSITION-STATE ANALOG.
    14. "Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding."
      Balendiran G.K., Molina J.A., Xu Y., Torres-Martinez J., Stevens R., Focia P.J., Eakin A.E., Sacchettini J.C., Craig S.P. III
      Protein Sci. 8:1023-1031(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT ALA-69 IN COMPLEX WITH PHOSPHORIBOSYLPYROPHOSPHATE; MAGNESIUM IONS AND HYPOXANTHINE ANALOG HPP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-69, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency."
      Sculley D.G., Dawson P.A., Emmerson B.T., Gordon R.B.
      Hum. Genet. 90:195-207(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    16. "The crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycle."
      Keough D.T., Brereton I.M., de Jersey J., Guddat L.W.
      J. Mol. Biol. 351:170-181(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF APOPROTEIN, SUBUNIT.
    17. "Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeutics."
      Keough D.T., Hockova D., Holy A., Naesens L.M., Skinner-Adams T.S., Jersey J., Guddat L.W.
      J. Med. Chem. 52:4391-4399(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEXES WITH ACYCLIC NUCLEOSIDE PHOSPHONATES, CATALYTIC ACTIVITY.
    18. "Human hypoxanthine-guanine phosphoribosyltransferase."
      Wilson J.M., Kobayashi R., Fox I.H., Kelley W.N.
      J. Biol. Chem. 258:6458-6460(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT TORONTO GLY-51.
    19. "Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome."
      Wilson J.M., Kelley W.N.
      J. Clin. Invest. 71:1331-1335(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS KINSTON ASN-194.
    20. "Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout."
      Wilson J.M., Tarr G.E., Kelley W.N.
      Proc. Natl. Acad. Sci. U.S.A. 80:870-873(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT LONDON LEU-110.
    21. "Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout."
      Wilson J.M., Kelley W.N.
      J. Biol. Chem. 259:27-30(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT MUNICH ARG-104.
    22. "Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich."
      Cariello N.F., Scott J.K., Kat A.G., Thilly W.G., Keohavong P.
      Am. J. Hum. Genet. 42:726-734(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT MUNICH ARG-104.
    23. "Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint)."
      Davidson B.L., Pashmforoush M., Kelly W.N., Palella T.D.
      Gene 63:331-336(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS FLINT LEU-74.
    24. "Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland)."
      Davidson B.L., Palella T.D., Kelly W.N.
      Gene 68:85-91(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS MIDLAND ASP-130.
    25. "Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor)."
      Fujimori S., Hidaka Y., Davidson B.L., Palella T.D., Kelley W.N.
      Hum. Genet. 79:39-43(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ANN ARBOR.
    26. "Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects."
      Davidson B.L., Chin S.J., Wilson J.M., Kelley W.N., Palella T.D.
      J. Clin. Invest. 82:2164-2167(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT LONDON LEU-110.
    27. "Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families."
      Keough D.T., Gordon R.B., Dejersey J., Emmerson B.T.
      J. Inherit. Metab. Dis. 11:229-238(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DIRRANBANDI AND YERONGA.
    28. "Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients."
      Igarashi T., Minami M., Nishida Y.
      Acta Paediatr. Jpn. Overseas Ed. 31:303-313(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS JAPAN-1 AND JAPAN-2.
    29. "Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville)."
      Davidson B.L., Pashmforoush M., Kelly W.N., Palella T.D.
      J. Biol. Chem. 264:520-525(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GOUT-HPRT ASHVILLE GLY-201.
    30. "Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome."
      Fujimori S., Davidson B.L., Kelley W.N., Palella T.D.
      J. Clin. Invest. 83:11-13(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS YALE ARG-71.
    31. "Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts."
      Davidson B.L., Tarle S.A., Palella T.D., Kelley W.N.
      J. Clin. Invest. 84:342-346(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARLINGEN; DETROIT; NEW BRITON AND NEW HAVEN.
    32. "Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA."
      Gibbs R.A., Nguyen P.N., McBride L.J., Koepf S.M., Caskey C.T.
      Proc. Natl. Acad. Sci. U.S.A. 86:1919-1923(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RKJ.
    33. "Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families."
      Gibbs R.A., Nguyen P.N., Edwards A., Civitello A.B., Caskey C.T.
      Genomics 7:235-244(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LNS RJK LYS-45; LEU-74; ASP-130; SER-131; LYS-143; SER-161; TYR-177; ASN-194; VAL-199; ASP-204 AND TYR-206.
    34. "Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures."
      Skopek T.R., Recio L., Simpson D., Dallaire L., Melancon S.B., Ogier H., O'Neill J.P., Falta M.T., Nicklas J.A., Albertini R.J.
      Hum. Genet. 85:111-116(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS MONTREAL THR-57.
    35. "Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE)."
      Gordon R.B., Sculley D.G., Dawson P.A., Beacham I.R., Emmerson B.T.
      J. Inherit. Metab. Dis. 13:692-700(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS BRISBANE ILE-168.
    36. "Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency."
      Davidson B.L., Tarle S.A., van Antwerp M., Gibbs D.A., Watts R.W.E., Kelley W.N., Palella T.D.
      Am. J. Hum. Genet. 48:951-958(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GRAVESEND; MASHAD; HEAPEY; BANBURY; RUNCORN; FARNHAM; MARLOW AND READING.
    37. "Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects."
      Tarle S.A., Davidson B.L., Wu V.C., Zidar F.J., Seegmiller J.E., Kelley W.N., Palella T.D.
      Genomics 10:499-501(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LNS TYR-28 DEL; VAL-50; GLU-70; LEU-74; THR-183 AND ARG-204.
    38. "Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification."
      Sculley D.G., Dawson P.A., Beacham I.R., Emmerson B.T., Gordon R.B.
      Hum. Genet. 87:688-692(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PERTH; SWAN; TOOWONG AND URANGAN.
    39. "Identification of two independent Japanese mutant HPRT genes using the PCR technique."
      Yamada Y., Goto H., Ogasawara N.
      Adv. Exp. Med. Biol. 309B:121-124(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALA-188, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 183-193.
    40. "The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction."
      Lightfoot T., Joshi R., Nuki G., Snyder F.F.
      Hum. Genet. 88:695-696(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDINBURGH GLY-52, NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    41. "Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency."
      Sege-Paterson K., Chambers J., Page T., Jones O.W., Nyhan W.L.
      Hum. Mol. Genet. 1:427-432(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS, NUCLEOTIDE SEQUENCE [MRNA] OF 35-50.
    42. Lightfoot T., Snyder F.F.
      Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: VARIANT GOUT-HPRT MOOSE JAW GLU-194, NUCLEOTIDE SEQUENCE.
    43. "Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies."
      Burgemeister R., Roetzer E., Gutensohn W., Gehrke M., Schiel W.
      Hum. Mutat. 5:341-344(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS ISAR PHE-42.
    44. "An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans."
      Fujimori S., Sakuma R., Yamaoka N., Hakoda M., Yamanaka H., Kamatani N.
      Hum. Genet. 99:8-10(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-61.
    45. "The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations."
      Liu G., Aral B., Zabot M.-T., Kamoun P., Ceballos-Picot I.
      Hum. Mutat. Suppl. 1:S88-S90(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LNS ROANNE VAL-177.

    Entry informationi

    Entry nameiHPRT_HUMAN
    AccessioniPrimary (citable) accession number: P00492
    Secondary accession number(s): A6NHF0, B2R8M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3