Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

HPRT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+Note: 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: IMP biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes IMP from hypoxanthine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Hypoxanthine-guanine phosphoribosyltransferase (HPRT1)
    This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from hypoxanthine, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei69GMP1 Publication1
    Active sitei138Proton acceptorCurated1
    Binding sitei166GMP1 Publication1
    Metal bindingi194Magnesium1
    Binding sitei194GMP; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi134 – 142GMP1 Publication9
    Nucleotide bindingi186 – 188GMP1 Publication3

    GO - Molecular functioni

    • guanine phosphoribosyltransferase activity Source: UniProtKB
    • hypoxanthine phosphoribosyltransferase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • nucleotide binding Source: UniProtKB-KW
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    • adenine salvage Source: GO_Central
    • central nervous system neuron development Source: Ensembl
    • cerebral cortex neuron differentiation Source: Ensembl
    • cytolysis Source: Ensembl
    • dendrite morphogenesis Source: Ensembl
    • dopamine metabolic process Source: Ensembl
    • GMP catabolic process Source: UniProtKB
    • GMP salvage Source: GO_Central
    • grooming behavior Source: Ensembl
    • guanine salvage Source: UniProtKB
    • hypoxanthine metabolic process Source: UniProtKB
    • hypoxanthine salvage Source: UniProtKB
    • IMP metabolic process Source: UniProtKB
    • IMP salvage Source: GO_Central
    • locomotory behavior Source: Ensembl
    • lymphocyte proliferation Source: Ensembl
    • positive regulation of dopamine metabolic process Source: UniProtKB
    • protein homotetramerization Source: UniProtKB
    • purine-containing compound salvage Source: Reactome
    • purine nucleotide biosynthetic process Source: UniProtKB
    • purine ribonucleoside salvage Source: UniProtKB
    • response to amphetamine Source: Ensembl
    • striatum development Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09275-MONOMER.
    ZFISH:HS09275-MONOMER.
    BRENDAi2.4.2.8. 2681.
    ReactomeiR-HSA-74217. 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
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:5157. HPRT1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: GO_Central
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Lesch-Nyhan syndrome (LNS)13 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionCharacterized by complete lack of enzymatic activity that results in hyperuricemia, choreoathetosis, mental retardation, and compulsive self-mutilation.
    See also OMIM:300322
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0067518V → G in LNS; HB. 1
    Natural variantiVAR_0716098Missing in LNS; Asia. 1 Publication1
    Natural variantiVAR_00675216G → D in LNS; FG. 1
    Natural variantiVAR_01231228Missing in LNS; Asia. 2 Publications1
    Natural variantiVAR_00675641L → P in LNS; Detroit. Corresponds to variant rs137852480dbSNPEnsembl.1
    Natural variantiVAR_00675742I → F in LNS; Isar. 1 Publication1
    Natural variantiVAR_00675842I → T in LNS; Heapey. 1
    Natural variantiVAR_00675943 – 44MD → RN in LNS; Salamanca. 2
    Natural variantiVAR_07161144D → Y in LNS; Japan. 1 Publication1
    Natural variantiVAR_00676045R → K in LNS; RJK 2163. 1 PublicationCorresponds to variant rs137852491dbSNPEnsembl.1
    Natural variantiVAR_00676350A → P in LNS; LW. 1
    Natural variantiVAR_00676250A → V in LNS; 1265. 1 Publication1
    Natural variantiVAR_00676551R → P in LNS; Banbury. 1
    Natural variantiVAR_00676954M → L in LNS; Japan-1. 1 Publication1
    Natural variantiVAR_00677057M → T in LNS; Montreal. 1 PublicationCorresponds to variant rs137852495dbSNPEnsembl.1
    Natural variantiVAR_07161364A → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_07161465L → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_00677370G → E in LNS; New Haven/1510, Asia. 3 PublicationsCorresponds to variant rs137852487dbSNPEnsembl.1
    Natural variantiVAR_00677471G → R in LNS; Yale. 1 PublicationCorresponds to variant rs137852488dbSNPEnsembl.1
    Natural variantiVAR_07161572Y → C in LNS; Asia. 2 Publications1
    Natural variantiVAR_00677574F → L in LNS; Flint/RJK 892/DW/Perth/1522, Japan. 4 PublicationsCorresponds to variant rs137852481dbSNPEnsembl.1
    Natural variantiVAR_07161678L → Q in LNS; Asia. 2 Publications1
    Natural variantiVAR_071617107 – 110Missing in LNS; Asia. 1 Publication4
    Natural variantiVAR_006780130V → D in LNS; Midland/RJK 896. 2 PublicationsCorresponds to variant rs137852483dbSNPEnsembl.1
    Natural variantiVAR_006781131L → S in LNS; RJK 1784. 1 Publication1
    Natural variantiVAR_006783132I → T in LNS; Runcorn. 1
    Natural variantiVAR_006785143M → K in LNS; RJK 1210. 1 PublicationCorresponds to variant rs137852496dbSNPEnsembl.1
    Natural variantiVAR_006786143M → MA in LNS; RW. 1
    Natural variantiVAR_071619147L → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_071620159K → E in LNS; Asia. 2 Publications1
    Natural variantiVAR_071621159K → KV in LNS; Asia. 1 Publication1
    Natural variantiVAR_006788162S → R in LNS; Farnham. 1
    Natural variantiVAR_006790176P → L in LNS; Marlow. Corresponds to variant rs137852493dbSNPEnsembl.1
    Natural variantiVAR_006791177D → V in LNS; Roanne. 1 Publication1
    Natural variantiVAR_006792177D → Y in LNS; RJK 2185. 1 PublicationCorresponds to variant rs137852492dbSNPEnsembl.1
    Natural variantiVAR_006793179Missing in LNS; Michigan. 1
    Natural variantiVAR_006795188V → A in GOUT-HPRT AND LNS; Asia. 3 Publications1
    Natural variantiVAR_006798194D → N in LNS; Kinston/RJK 2188. 2 PublicationsCorresponds to variant rs267606863dbSNPEnsembl.1
    Natural variantiVAR_006800199F → V in LNS; New Briton/RJK 950. 1 PublicationCorresponds to variant rs137852486dbSNPEnsembl.1
    Natural variantiVAR_006803201D → Y in LNS; GM. 1
    Natural variantiVAR_006804204H → D in LNS; RJK 1874. 1 PublicationCorresponds to variant rs137852490dbSNPEnsembl.1
    Natural variantiVAR_006805204H → R in LNS; 779. 1 Publication1
    Natural variantiVAR_006806206C → Y in LNS; Reading/RJK 1727. 1 Publication1
    Gout HPRT-related (GOUT-HPRT)11 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionCharacterized by partial enzyme activity and hyperuricemia.
    See also OMIM:300323
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0067507G → D in GOUT-HPRT; Gravesend. 1
    Natural variantiVAR_00675316G → S in GOUT-HPRT; Urangan. Corresponds to variant rs137852499dbSNPEnsembl.1
    Natural variantiVAR_00675420D → V in GOUT-HPRT; Mashad; strongly reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_07161023C → F in GOUT-HPRT; Reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_00675523C → W in GOUT-HPRT; JS. 1
    Natural variantiVAR_00676148R → H in GOUT-HPRT; AD and DD. Corresponds to variant rs387906725dbSNPEnsembl.1
    Natural variantiVAR_00676451R → G in GOUT-HPRT; Toronto. 1 PublicationCorresponds to variant rs137852494dbSNPEnsembl.1
    Natural variantiVAR_00676753V → A in GOUT-HPRT; MG. 1
    Natural variantiVAR_00676853V → M in GOUT-HPRT; TE. 1
    Natural variantiVAR_00677158G → R in GOUT-HPRT; Toowong. Corresponds to variant rs137852500dbSNPEnsembl.1
    Natural variantiVAR_07161260H → R in GOUT-HPRT; Reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_00677678L → V in GOUT-HPRT; Swan. Corresponds to variant rs137852501dbSNPEnsembl.1
    Natural variantiVAR_00677780D → V in GOUT-HPRT; Arlington. Corresponds to variant rs137852478dbSNPEnsembl.1
    Natural variantiVAR_006778104S → R in GOUT-HPRT; Munich. 2 PublicationsCorresponds to variant rs137852485dbSNPEnsembl.1
    Natural variantiVAR_006779110S → L in GOUT-HPRT; London. 2 PublicationsCorresponds to variant rs137852482dbSNPEnsembl.1
    Natural variantiVAR_071618124T → P in GOUT-HPRT; Asia. 1 Publication1
    Natural variantiVAR_006782132I → M in GOUT-HPRT; Ann-Arbor. 1 PublicationCorresponds to variant rs137852477dbSNPEnsembl.1
    Natural variantiVAR_006784135D → G in GOUT-HPRT; Yeronga. 1
    Natural variantiVAR_006787161A → S in GOUT-HPRT; Milwaukee/RJK 949. 1 PublicationCorresponds to variant rs137852484dbSNPEnsembl.1
    Natural variantiVAR_006789168T → I in GOUT-HPRT; Brisbane. 1 PublicationCorresponds to variant rs137852498dbSNPEnsembl.1
    Natural variantiVAR_006794179 – 180VG → GR in GOUT-HPRT; Japan-2. 2
    Natural variantiVAR_006796183I → T in GOUT-HPRT; JF. 1 Publication1
    Natural variantiVAR_071622185D → G in GOUT-HPRT; Asia. 1 Publication1
    Natural variantiVAR_006795188V → A in GOUT-HPRT AND LNS; Asia. 3 Publications1
    Natural variantiVAR_071623192A → V in GOUT-HPRT; Asia. 2 Publications1
    Natural variantiVAR_006797194D → E in GOUT-HPRT; Moose-Jaw; results in cooperativity and decreased substrate affinities. 1 PublicationCorresponds to variant rs137852504dbSNPEnsembl.1
    Natural variantiVAR_006799195Y → C in GOUT-HPRT; Dirranbandi, Asia. 2 Publications1
    Natural variantiVAR_006801201D → G in GOUT-HPRT; Ashville. 1 PublicationCorresponds to variant rs137852479dbSNPEnsembl.1
    Natural variantiVAR_006802201D → N in GOUT-HPRT; RB. 1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi69K → A: Reduced affinity for hypoxanthine, phosphoribosylpyrophosphate and IMP. Reduced catalytic activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Gout

    Organism-specific databases

    DisGeNETi3251.
    MalaCardsiHPRT1.
    MIMi300322. phenotype.
    300323. phenotype.
    OpenTargetsiENSG00000165704.
    Orphaneti79233. Hypoxanthine guanine phosphoribosyltransferase partial deficiency.
    510. Lesch-Nyhan syndrome.
    PharmGKBiPA29427.

    Chemistry databases

    ChEMBLiCHEMBL2360.
    DrugBankiDB00993. Azathioprine.
    DB01033. Mercaptopurine.
    DB00352. Tioguanine.

    Polymorphism and mutation databases

    BioMutaiHPRT1.
    DMDMi123497.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001395852 – 218Hypoxanthine-guanine phosphoribosyltransferaseAdd BLAST217

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanine1 Publication1
    Modified residuei103N6-acetyllysineBy similarity1
    Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
    Modified residuei142PhosphothreonineBy similarity1

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP00492.
    MaxQBiP00492.
    PaxDbiP00492.
    PeptideAtlasiP00492.
    PRIDEiP00492.
    TopDownProteomicsiP00492.

    2D gel databases

    OGPiP00492.
    REPRODUCTION-2DPAGEIPI00218493.

    PTM databases

    iPTMnetiP00492.
    PhosphoSitePlusiP00492.
    SwissPalmiP00492.

    Expressioni

    Gene expression databases

    BgeeiENSG00000165704.
    CleanExiHS_HPRT1.
    ExpressionAtlasiP00492. baseline and differential.
    GenevisibleiP00492. HS.

    Organism-specific databases

    HPAiCAB012200.
    HPA006360.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-748210,EBI-748210
    ISCUQ9H1K13EBI-748210,EBI-1047335
    PRTFDC1Q9NRG14EBI-748210,EBI-739759
    SDCBPO005605EBI-748210,EBI-727004
    WDYHV1Q96HA88EBI-748210,EBI-741158

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi109488. 27 interactors.
    IntActiP00492. 11 interactors.
    MINTiMINT-1443310.
    STRINGi9606.ENSP00000298556.

    Chemistry databases

    BindingDBiP00492.

    Structurei

    Secondary structure

    1218
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 9Combined sources3
    Beta strandi12 – 14Combined sources3
    Helixi19 – 21Combined sources3
    Helixi26 – 28Combined sources3
    Turni29 – 31Combined sources3
    Beta strandi32 – 37Combined sources6
    Helixi39 – 57Combined sources19
    Beta strandi62 – 68Combined sources7
    Turni69 – 71Combined sources3
    Helixi72 – 87Combined sources16
    Beta strandi89 – 91Combined sources3
    Beta strandi95 – 101Combined sources7
    Beta strandi109 – 118Combined sources10
    Helixi119 – 121Combined sources3
    Helixi123 – 125Combined sources3
    Beta strandi128 – 140Combined sources13
    Helixi141 – 150Combined sources10
    Helixi151 – 153Combined sources3
    Beta strandi156 – 166Combined sources11
    Beta strandi169 – 171Combined sources3
    Beta strandi177 – 183Combined sources7
    Beta strandi188 – 190Combined sources3
    Beta strandi195 – 197Combined sources3
    Beta strandi198 – 201Combined sources4
    Beta strandi203 – 208Combined sources6
    Helixi210 – 216Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4RABX-ray2.26A/B/C/D2-218[»]
    4RACX-ray2.05A/B/C/D2-218[»]
    4RADX-ray2.00A/B/C/D/E/F/G/H2-218[»]
    4RANX-ray2.55A/B/C/D2-218[»]
    4RAOX-ray1.87A/B/C/D2-218[»]
    4RAQX-ray2.53A/B/C/D2-218[»]
    5BRNX-ray2.30A/B/C/D1-218[»]
    5BSKX-ray2.61A/B/C/D1-218[»]
    ProteinModelPortaliP00492.
    SMRiP00492.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00492.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG3367. Eukaryota.
    COG0634. LUCA.
    GeneTreeiENSGT00390000017323.
    HOGENOMiHOG000236521.
    HOVERGENiHBG000242.
    InParanoidiP00492.
    KOiK00760.
    OMAiDIAYVGF.
    OrthoDBiEOG091G0K6K.
    PhylomeDBiP00492.
    TreeFamiTF313367.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    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

            10         20         30         40         50
    MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA
    60 70 80 90 100
    RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI
    110 120 130 140 150
    RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV
    160 170 180 190 200
    RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR
    210
    DLNHVCVISE TGKAKYKA
    Length:218
    Mass (Da):24,579
    Last modified:January 23, 2007 - v2
    Checksum:i1928EE69517CCB40
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0067507G → D in GOUT-HPRT; Gravesend. 1
    Natural variantiVAR_0067518V → G in LNS; HB. 1
    Natural variantiVAR_0716098Missing in LNS; Asia. 1 Publication1
    Natural variantiVAR_00675216G → D in LNS; FG. 1
    Natural variantiVAR_00675316G → S in GOUT-HPRT; Urangan. Corresponds to variant rs137852499dbSNPEnsembl.1
    Natural variantiVAR_00675420D → V in GOUT-HPRT; Mashad; strongly reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_07161023C → F in GOUT-HPRT; Reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_00675523C → W in GOUT-HPRT; JS. 1
    Natural variantiVAR_01231228Missing in LNS; Asia. 2 Publications1
    Natural variantiVAR_00675641L → P in LNS; Detroit. Corresponds to variant rs137852480dbSNPEnsembl.1
    Natural variantiVAR_00675742I → F in LNS; Isar. 1 Publication1
    Natural variantiVAR_00675842I → T in LNS; Heapey. 1
    Natural variantiVAR_00675943 – 44MD → RN in LNS; Salamanca. 2
    Natural variantiVAR_07161144D → Y in LNS; Japan. 1 Publication1
    Natural variantiVAR_00676045R → K in LNS; RJK 2163. 1 PublicationCorresponds to variant rs137852491dbSNPEnsembl.1
    Natural variantiVAR_00676148R → H in GOUT-HPRT; AD and DD. Corresponds to variant rs387906725dbSNPEnsembl.1
    Natural variantiVAR_00676350A → P in LNS; LW. 1
    Natural variantiVAR_00676250A → V in LNS; 1265. 1 Publication1
    Natural variantiVAR_00676451R → G in GOUT-HPRT; Toronto. 1 PublicationCorresponds to variant rs137852494dbSNPEnsembl.1
    Natural variantiVAR_00676551R → P in LNS; Banbury. 1
    Natural variantiVAR_00676652D → G in Edinburgh. 1 PublicationCorresponds to variant rs137852502dbSNPEnsembl.1
    Natural variantiVAR_00676753V → A in GOUT-HPRT; MG. 1
    Natural variantiVAR_00676853V → M in GOUT-HPRT; TE. 1
    Natural variantiVAR_00676954M → L in LNS; Japan-1. 1 Publication1
    Natural variantiVAR_00677057M → T in LNS; Montreal. 1 PublicationCorresponds to variant rs137852495dbSNPEnsembl.1
    Natural variantiVAR_00677158G → R in GOUT-HPRT; Toowong. Corresponds to variant rs137852500dbSNPEnsembl.1
    Natural variantiVAR_07161260H → R in GOUT-HPRT; Reduces enzymatic activity. 1 Publication1
    Natural variantiVAR_00677261H → R Enzyme activity 37% of normal; asymptomatic. 1 Publication1
    Natural variantiVAR_07161364A → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_07161465L → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_00677370G → E in LNS; New Haven/1510, Asia. 3 PublicationsCorresponds to variant rs137852487dbSNPEnsembl.1
    Natural variantiVAR_00677471G → R in LNS; Yale. 1 PublicationCorresponds to variant rs137852488dbSNPEnsembl.1
    Natural variantiVAR_07161572Y → C in LNS; Asia. 2 Publications1
    Natural variantiVAR_00677574F → L in LNS; Flint/RJK 892/DW/Perth/1522, Japan. 4 PublicationsCorresponds to variant rs137852481dbSNPEnsembl.1
    Natural variantiVAR_07161678L → Q in LNS; Asia. 2 Publications1
    Natural variantiVAR_00677678L → V in GOUT-HPRT; Swan. Corresponds to variant rs137852501dbSNPEnsembl.1
    Natural variantiVAR_00677780D → V in GOUT-HPRT; Arlington. Corresponds to variant rs137852478dbSNPEnsembl.1
    Natural variantiVAR_006778104S → R in GOUT-HPRT; Munich. 2 PublicationsCorresponds to variant rs137852485dbSNPEnsembl.1
    Natural variantiVAR_071617107 – 110Missing in LNS; Asia. 1 Publication4
    Natural variantiVAR_006779110S → L in GOUT-HPRT; London. 2 PublicationsCorresponds to variant rs137852482dbSNPEnsembl.1
    Natural variantiVAR_071618124T → P in GOUT-HPRT; Asia. 1 Publication1
    Natural variantiVAR_006780130V → D in LNS; Midland/RJK 896. 2 PublicationsCorresponds to variant rs137852483dbSNPEnsembl.1
    Natural variantiVAR_006781131L → S in LNS; RJK 1784. 1 Publication1
    Natural variantiVAR_006782132I → M in GOUT-HPRT; Ann-Arbor. 1 PublicationCorresponds to variant rs137852477dbSNPEnsembl.1
    Natural variantiVAR_006783132I → T in LNS; Runcorn. 1
    Natural variantiVAR_006784135D → G in GOUT-HPRT; Yeronga. 1
    Natural variantiVAR_006785143M → K in LNS; RJK 1210. 1 PublicationCorresponds to variant rs137852496dbSNPEnsembl.1
    Natural variantiVAR_006786143M → MA in LNS; RW. 1
    Natural variantiVAR_071619147L → P in LNS; Asia. 2 Publications1
    Natural variantiVAR_071620159K → E in LNS; Asia. 2 Publications1
    Natural variantiVAR_071621159K → KV in LNS; Asia. 1 Publication1
    Natural variantiVAR_006787161A → S in GOUT-HPRT; Milwaukee/RJK 949. 1 PublicationCorresponds to variant rs137852484dbSNPEnsembl.1
    Natural variantiVAR_006788162S → R in LNS; Farnham. 1
    Natural variantiVAR_006789168T → I in GOUT-HPRT; Brisbane. 1 PublicationCorresponds to variant rs137852498dbSNPEnsembl.1
    Natural variantiVAR_006790176P → L in LNS; Marlow. Corresponds to variant rs137852493dbSNPEnsembl.1
    Natural variantiVAR_006791177D → V in LNS; Roanne. 1 Publication1
    Natural variantiVAR_006792177D → Y in LNS; RJK 2185. 1 PublicationCorresponds to variant rs137852492dbSNPEnsembl.1
    Natural variantiVAR_006794179 – 180VG → GR in GOUT-HPRT; Japan-2. 2
    Natural variantiVAR_006793179Missing in LNS; Michigan. 1
    Natural variantiVAR_006796183I → T in GOUT-HPRT; JF. 1 Publication1
    Natural variantiVAR_071622185D → G in GOUT-HPRT; Asia. 1 Publication1
    Natural variantiVAR_006795188V → A in GOUT-HPRT AND LNS; Asia. 3 Publications1
    Natural variantiVAR_071623192A → V in GOUT-HPRT; Asia. 2 Publications1
    Natural variantiVAR_006797194D → E in GOUT-HPRT; Moose-Jaw; results in cooperativity and decreased substrate affinities. 1 PublicationCorresponds to variant rs137852504dbSNPEnsembl.1
    Natural variantiVAR_006798194D → N in LNS; Kinston/RJK 2188. 2 PublicationsCorresponds to variant rs267606863dbSNPEnsembl.1
    Natural variantiVAR_006799195Y → C in GOUT-HPRT; Dirranbandi, Asia. 2 Publications1
    Natural variantiVAR_006800199F → V in LNS; New Briton/RJK 950. 1 PublicationCorresponds to variant rs137852486dbSNPEnsembl.1
    Natural variantiVAR_006801201D → G in GOUT-HPRT; Ashville. 1 PublicationCorresponds to variant rs137852479dbSNPEnsembl.1
    Natural variantiVAR_006802201D → N in GOUT-HPRT; RB. 1
    Natural variantiVAR_006803201D → Y in LNS; GM. 1
    Natural variantiVAR_006804204H → D in LNS; RJK 1874. 1 PublicationCorresponds to variant rs137852490dbSNPEnsembl.1
    Natural variantiVAR_006805204H → R in LNS; 779. 1 Publication1
    Natural variantiVAR_006806206C → Y in LNS; Reading/RJK 1727. 1 Publication1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.5. human.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Hypoxanthine-guanine phosphoribosyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4RABX-ray2.26A/B/C/D2-218[»]
    4RACX-ray2.05A/B/C/D2-218[»]
    4RADX-ray2.00A/B/C/D/E/F/G/H2-218[»]
    4RANX-ray2.55A/B/C/D2-218[»]
    4RAOX-ray1.87A/B/C/D2-218[»]
    4RAQX-ray2.53A/B/C/D2-218[»]
    5BRNX-ray2.30A/B/C/D1-218[»]
    5BSKX-ray2.61A/B/C/D1-218[»]
    ProteinModelPortaliP00492.
    SMRiP00492.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109488. 27 interactors.
    IntActiP00492. 11 interactors.
    MINTiMINT-1443310.
    STRINGi9606.ENSP00000298556.

    Chemistry databases

    BindingDBiP00492.
    ChEMBLiCHEMBL2360.
    DrugBankiDB00993. Azathioprine.
    DB01033. Mercaptopurine.
    DB00352. Tioguanine.

    PTM databases

    iPTMnetiP00492.
    PhosphoSitePlusiP00492.
    SwissPalmiP00492.

    Polymorphism and mutation databases

    BioMutaiHPRT1.
    DMDMi123497.

    2D gel databases

    OGPiP00492.
    REPRODUCTION-2DPAGEIPI00218493.

    Proteomic databases

    EPDiP00492.
    MaxQBiP00492.
    PaxDbiP00492.
    PeptideAtlasiP00492.
    PRIDEiP00492.
    TopDownProteomicsiP00492.

    Protocols and materials databases

    DNASUi3251.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000298556; ENSP00000298556; ENSG00000165704.
    GeneIDi3251.
    KEGGihsa:3251.
    UCSCiuc004exl.5. human.

    Organism-specific databases

    CTDi3251.
    DisGeNETi3251.
    GeneCardsiHPRT1.
    GeneReviewsiHPRT1.
    HGNCiHGNC:5157. HPRT1.
    HPAiCAB012200.
    HPA006360.
    MalaCardsiHPRT1.
    MIMi300322. phenotype.
    300323. phenotype.
    308000. gene.
    neXtProtiNX_P00492.
    OpenTargetsiENSG00000165704.
    Orphaneti79233. Hypoxanthine guanine phosphoribosyltransferase partial deficiency.
    510. Lesch-Nyhan syndrome.
    PharmGKBiPA29427.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3367. Eukaryota.
    COG0634. LUCA.
    GeneTreeiENSGT00390000017323.
    HOGENOMiHOG000236521.
    HOVERGENiHBG000242.
    InParanoidiP00492.
    KOiK00760.
    OMAiDIAYVGF.
    OrthoDBiEOG091G0K6K.
    PhylomeDBiP00492.
    TreeFamiTF313367.

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00648.
    BioCyciMetaCyc:HS09275-MONOMER.
    ZFISH:HS09275-MONOMER.
    BRENDAi2.4.2.8. 2681.
    ReactomeiR-HSA-74217. Purine salvage.
    SABIO-RKP00492.

    Miscellaneous databases

    ChiTaRSiHPRT1. human.
    EvolutionaryTraceiP00492.
    GeneWikiiHypoxanthine-guanine_phosphoribosyltransferase.
    GenomeRNAii3251.
    PROiP00492.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000165704.
    CleanExiHS_HPRT1.
    ExpressionAtlasiP00492. baseline and differential.
    GenevisibleiP00492. HS.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    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]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 193 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.