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P00492

- HPRT_HUMAN

UniProt

P00492 - HPRT_HUMAN

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Protein
Hypoxanthine-guanine phosphoribosyltransferase
Gene
HPRT1, HPRT
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications
GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications

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 hypoxanthine
  3. KM=25 µM for pyrophosphate
  4. KM=31 µM for phosphoribosylpyrophosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691GMP
Active sitei138 – 1381Proton acceptor Inferred
Binding sitei166 – 1661GMP
Metal bindingi194 – 1941Magnesium
Binding sitei194 – 1941GMP; via carbonyl oxygen

Regions

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

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
Complete GO annotation...

GO - Biological processi

  1. GMP catabolic process Source: UniProtKB
  2. GMP salvage Source: RefGenome
  3. IMP metabolic process Source: UniProtKB
  4. IMP salvage Source: RefGenome
  5. adenine salvage Source: RefGenome
  6. central nervous system neuron development Source: Ensembl
  7. cerebral cortex neuron differentiation Source: Ensembl
  8. cytolysis Source: Ensembl
  9. dendrite morphogenesis Source: Ensembl
  10. dopamine metabolic process Source: Ensembl
  11. grooming behavior Source: Ensembl
  12. guanine salvage Source: UniProtKB
  13. hypoxanthine metabolic process Source: UniProtKB
  14. hypoxanthine salvage Source: UniProtKB
  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 nucleobase metabolic process Source: Reactome
  21. purine nucleotide biosynthetic process Source: UniProtKB
  22. purine ribonucleoside salvage Source: UniProtKB
  23. purine-containing compound salvage Source: Reactome
  24. response to amphetamine Source: Ensembl
  25. small molecule metabolic process Source: Reactome
  26. 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.
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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
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 phosphoribosyltransferase
PRO_0000139585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei103 – 1031N6-acetyllysine By 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.1 Publication

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

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.

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

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