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P00492 (HPRT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypoxanthine-guanine phosphoribosyltransferase

Short name=HGPRT
Short name=HGPRTase
EC=2.4.2.8
Gene names
Name:HPRT1
Synonyms:HPRT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.14 Ref.17

GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.14 Ref.17

Cofactor

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

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.

Subunit structure

Homotetramer. Ref.16

Subcellular location

Cytoplasm.

Involvement in disease

Lesch-Nyhan syndrome (LNS) [MIM:300322]: Characterized by complete lack of enzymatic activity that results in hyperuricemia, choreoathetosis, mental retardation, and compulsive self-mutilation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.23 Ref.24 Ref.30 Ref.33 Ref.34 Ref.35 Ref.37 Ref.43 Ref.45

Gout HPRT-related (GOUT-HPRT) [MIM:300323]: Characterized by partial enzyme activity and hyperuricemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.20 Ref.21 Ref.22 Ref.26 Ref.29 Ref.42

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=5.4 µM for IMP Ref.14

KM=0.45 µM for hypoxanthine

KM=25 µM for pyrophosphate

KM=31 µM for phosphoribosylpyrophosphate

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   DiseaseDisease mutation
Gout
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGMP catabolic process

Inferred from direct assay Ref.17. Source: UniProtKB

GMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

IMP metabolic process

Inferred from direct assay Ref.17. Source: UniProtKB

IMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenine salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

behavior

Inferred from mutant phenotype. Source: UniProtKB

central nervous system neuron development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex neuron differentiation

Inferred from electronic annotation. Source: Ensembl

cytolysis

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

grooming behavior

Inferred from electronic annotation. Source: Ensembl

guanine salvage

Inferred from direct assay Ref.17. Source: UniProtKB

hypoxanthine metabolic process

Inferred from mutant phenotype PubMed 9824441. Source: UniProtKB

hypoxanthine salvage

Inferred from direct assay Ref.17. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

lymphocyte proliferation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

positive regulation of dopamine metabolic process

Inferred from mutant phenotype PubMed 8643611. Source: UniProtKB

protein homotetramerization

Inferred from direct assay PubMed 9521733. Source: UniProtKB

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine nucleotide biosynthetic process

Inferred from mutant phenotype PubMed 9824441. Source: UniProtKB

purine ribonucleoside salvage

Inferred from mutant phenotype PubMed 9824441. Source: UniProtKB

purine-containing compound salvage

Traceable author statement. Source: Reactome

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

striatum development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionguanine phosphoribosyltransferase activity

Inferred from direct assay Ref.17. Source: UniProtKB

hypoxanthine phosphoribosyltransferase activity

Inferred from direct assay Ref.17Ref.1PubMed 9521733. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WDYHV1Q96HA83EBI-748210,EBI-741158

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 218217Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139585

Regions

Nucleotide binding134 – 1429GMP
Nucleotide binding186 – 1883GMP

Sites

Active site1381Proton acceptor Probable
Metal binding1941Magnesium
Binding site691GMP
Binding site1661GMP
Binding site1941GMP; via carbonyl oxygen

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue1031N6-acetyllysine By similarity

Natural variations

Natural variant71G → D in GOUT-HPRT; Gravesend.
VAR_006750
Natural variant81V → G in LNS; HB.
VAR_006751
Natural variant161G → D in LNS; FG.
VAR_006752
Natural variant161G → S in GOUT-HPRT; Urangan.
VAR_006753
Natural variant201D → V in GOUT-HPRT; Mashad.
VAR_006754
Natural variant231C → W in GOUT-HPRT; JS.
VAR_006755
Natural variant281Missing in LNS. Ref.37
VAR_012312
Natural variant411L → P in LNS; Detroit.
VAR_006756
Natural variant421I → F in LNS; Isar. Ref.43
VAR_006757
Natural variant421I → T in LNS; Heapey.
VAR_006758
Natural variant43 – 442MD → RN in LNS; Salamanca.
VAR_006759
Natural variant451R → K in LNS; RJK 2163. Ref.33
VAR_006760
Natural variant481R → H in GOUT-HPRT; AD and DD.
VAR_006761
Natural variant501A → P in LNS; LW.
VAR_006763
Natural variant501A → V in LNS; 1265. Ref.37
VAR_006762
Natural variant511R → G in GOUT-HPRT; Toronto. Ref.18
VAR_006764
Natural variant511R → P in LNS; Banbury.
VAR_006765
Natural variant521D → G in Edinburgh. Ref.40
VAR_006766
Natural variant531V → A in GOUT-HPRT; MG.
VAR_006767
Natural variant531V → M in GOUT-HPRT; TE.
VAR_006768
Natural variant541M → L in LNS; Japan-1.
VAR_006769
Natural variant571M → T in LNS; Montreal. Ref.34
VAR_006770
Natural variant581G → R in GOUT-HPRT; Toowong.
VAR_006771
Natural variant611H → R Enzyme activity 37% of normal; asymptomatic. Ref.44
VAR_006772
Natural variant701G → E in LNS; New Haven/1510. Ref.37
VAR_006773
Natural variant711G → R in LNS; Yale. Ref.30
VAR_006774
Natural variant741F → L in LNS; Flint/RJK 892/DW/Perth/1522. Ref.23 Ref.33 Ref.37
VAR_006775
Natural variant781L → V in GOUT-HPRT; Swan.
VAR_006776
Natural variant801D → V in GOUT-HPRT; Arlington.
VAR_006777
Natural variant1041S → R in GOUT-HPRT; Munich. Ref.21 Ref.22
VAR_006778
Natural variant1101S → L in GOUT-HPRT; London. Ref.20 Ref.26
VAR_006779
Natural variant1301V → D in LNS; Midland/RJK 896. Ref.24 Ref.33
VAR_006780
Natural variant1311L → S in LNS; RJK 1784. Ref.33
VAR_006781
Natural variant1321I → M in GOUT-HPRT; Ann-Arbor.
VAR_006782
Natural variant1321I → T in LNS; Runcorn.
VAR_006783
Natural variant1351D → G in GOUT-HPRT; Yeronga.
VAR_006784
Natural variant1431M → K in LNS; RJK 1210. Ref.33
VAR_006785
Natural variant1431M → MA in LNS; RW.
VAR_006786
Natural variant1611A → S in GOUT-HPRT; Milwaukee/RJK 949. Ref.33
VAR_006787
Natural variant1621S → R in LNS; Farnham.
VAR_006788
Natural variant1681T → I in GOUT-HPRT; Brisbane. Ref.35
VAR_006789
Natural variant1761P → L in LNS; Marlow.
VAR_006790
Natural variant1771D → V in LNS; Roanne. Ref.45
VAR_006791
Natural variant1771D → Y in LNS; RJK 2185. Ref.33
VAR_006792
Natural variant179 – 1802VG → GR in GOUT-HPRT; Japan-2.
VAR_006794
Natural variant1791Missing in LNS; Michigan.
VAR_006793
Natural variant1831I → T in GOUT-HPRT; JF. Ref.37
VAR_006796
Natural variant1881V → A in Japan. Ref.39
VAR_006795
Natural variant1941D → E in GOUT-HPRT; Moose-Jaw; results in cooperativity and decreased substrate affinities. Ref.42
VAR_006797
Natural variant1941D → N in LNS; Kinston/RJK 2188. Ref.19 Ref.33
VAR_006798
Natural variant1951Y → C in GOUT-HPRT; Dirranbandi.
VAR_006799
Natural variant1991F → V in LNS; New Briton/RJK 950. Ref.33
VAR_006800
Natural variant2011D → G in GOUT-HPRT; Ashville. Ref.29
VAR_006801
Natural variant2011D → N in GOUT-HPRT; RB.
VAR_006802
Natural variant2011D → Y in LNS; GM.
VAR_006803
Natural variant2041H → D in LNS; RJK 1874. Ref.33
VAR_006804
Natural variant2041H → R in LNS; 779. Ref.37
VAR_006805
Natural variant2061C → Y in LNS; Reading/RJK 1727. Ref.33
VAR_006806

Experimental info

Mutagenesis691K → A: Reduced affinity for hypoxanthine, phosphoribosylpyrophosphate and IMP. Reduced catalytic activity. Ref.14

Secondary structure

............................................ 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00492 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1928EE69517CCB40

FASTA21824,579
        10         20         30         40         50         60 
MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH 

        70         80         90        100        110        120 
HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD 

       130        140        150        160        170        180 
DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG 

       190        200        210 
FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA 

« Hide

References

« Hide 'large scale' references
[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]"Automated DNA sequencing of the human HPRT locus."
Edwards A., Voss H., Rice P., Civitello A., Stegemann J., Schwager C., Zimmermann J., Erfle H., Caskey C.T., Ansorge W.
Genomics 6:593-608(1990) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

GeneReviews
NIEHS-SNPs
Wikipedia

Hypoxanthine-guanine phosphoribosyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRTHUG. A32728.
RefSeqNP_000185.1. NM_000194.2.
UniGeneHs.412707.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D2-217[»]
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[»]
ProteinModelPortalP00492.
SMRP00492. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109488. 21 interactions.
IntActP00492. 4 interactions.
MINTMINT-1443310.
STRING9606.ENSP00000298556.

Chemistry

BindingDBP00492.
ChEMBLCHEMBL2360.
DrugBankDB01033. Mercaptopurine.
DB00352. Thioguanine.

PTM databases

PhosphoSiteP00492.

Polymorphism databases

DMDM123497.

2D gel databases

OGPP00492.
REPRODUCTION-2DPAGEIPI00218493.

Proteomic databases

PaxDbP00492.
PeptideAtlasP00492.
PRIDEP00492.

Protocols and materials databases

DNASU3251.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298556; ENSP00000298556; ENSG00000165704.
GeneID3251.
KEGGhsa:3251.
UCSCuc004exl.4. human.

Organism-specific databases

CTD3251.
GeneCardsGC0XP133594.
HGNCHGNC:5157. HPRT1.
HPACAB012200.
HPA006360.
MIM300322. phenotype.
300323. phenotype.
308000. gene.
neXtProtNX_P00492.
Orphanet79233. Kelley-Seegmiller syndrome.
510. Lesch-Nyhan syndrome.
PharmGKBPA29427.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000236521.
HOVERGENHBG000242.
KOK00760.
OMALIMDSRT.
OrthoDBEOG7673CK.
PhylomeDBP00492.
TreeFamTF313367.

Enzyme and pathway databases

BioCycMetaCyc:HS09275-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00492.
UniPathwayUPA00591; UER00648.

Gene expression databases

BgeeP00492.
CleanExHS_HPRT1.
GenevestigatorP00492.

Family and domain databases

InterProIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHPRT1. human.
EvolutionaryTraceP00492.
GeneWikiHypoxanthine-guanine_phosphoribosyltransferase.
GenomeRNAi3251.
NextBio12927.
PROP00492.
SOURCESearch...

Entry information

Entry nameHPRT_HUMAN
AccessionPrimary (citable) accession number: P00492
Secondary accession number(s): A6NHF0, B2R8M9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM