HUMAN:HPRT

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HPRT1 (synonyms: HPRT)
Protein Name(s)	Hypoxanthine-guanine phosphoribosyltransferase HGPRT HGPRTase
External Links
UniProt	P00492
EMBL	M31642 M26434 AK313435 BT019350 AY780550 AC004383 CH471107 BC000578 M12452 S79313 L29383 L29382 S60300
CCDS	CCDS14641.1
PIR	A32728
RefSeq	NP_000185.1
UniGene	Hs.412707
PDB	1BZY 1D6N 1HMP 1Z7G 2VFA 3GEP 3GGC 3GGJ 4IJQ 4KN6
PDBsum	1BZY 1D6N 1HMP 1Z7G 2VFA 3GEP 3GGC 3GGJ 4IJQ 4KN6
ProteinModelPortal	P00492
SMR	P00492
BioGrid	109488
IntAct	P00492
MINT	MINT-1443310
STRING	9606.ENSP00000298556
BindingDB	P00492
ChEMBL	CHEMBL2360
DrugBank	DB00993 DB01033 DB00352
PhosphoSite	P00492
DMDM	123497
OGP	P00492
REPRODUCTION-2DPAGE	IPI00218493
MaxQB	P00492
PaxDb	P00492
PeptideAtlas	P00492
PRIDE	P00492
DNASU	3251
Ensembl	ENST00000298556
GeneID	3251
KEGG	hsa:3251
UCSC	uc004exl.4
CTD	3251
GeneCards	GC0XP133594
GeneReviews	HPRT1
HGNC	HGNC:5157
HPA	CAB012200 HPA006360
MIM	300322 300323 308000
neXtProt	NX_P00492
Orphanet	79233 510
PharmGKB	PA29427
eggNOG	COG0634
GeneTree	ENSGT00390000017323
HOGENOM	HOG000236521
HOVERGEN	HBG000242
InParanoid	P00492
KO	K00760
OMA	EMQWRVA
OrthoDB	EOG7673CK
PhylomeDB	P00492
TreeFam	TF313367
BioCyc	MetaCyc:HS09275-MONOMER
Reactome	REACT_1923
SABIO-RK	P00492
UniPathway	UPA00591
ChiTaRS	HPRT1
EvolutionaryTrace	P00492
GeneWiki	Hypoxanthine-guanine_phosphoribosyltransferase
GenomeRNAi	3251
NextBio	12927
PRO	PR:P00492
Proteomes	UP000005640
Bgee	P00492
CleanEx	HS_HPRT1
Genevestigator	P00492
GO	GO:0005737 GO:0005829 GO:0070062 GO:0052657 GO:0004422 GO:0000287 GO:0000166 GO:0042803 GO:0006168 GO:0021954 GO:0021895 GO:0019835 GO:0048813 GO:0042417 GO:0046038 GO:0032263 GO:0007625 GO:0006178 GO:0046100 GO:0043103 GO:0046040 GO:0032264 GO:0007626 GO:0046651 GO:0055086 GO:0045964 GO:0051289 GO:0006144 GO:0006164 GO:0006166 GO:0043101 GO:0001975 GO:0044281 GO:0021756
Gene3D	3.40.50.2020
InterPro	IPR005904 IPR000836 IPR029057
Pfam	PF00156
SUPFAM	SSF53271
TIGRFAMs	TIGR01203
PROSITE	PS00103

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0070062	extracellular exosome	PMID:20458337^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
enables	GO:0052657	guanine phosphoribosyltransferase activity	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
	GO:0000100	S-methylmethionine transmembrane transporter activity	PMID:17662107^[3]	ECO:0000250		UniProtKB:Q8R7L0	F		The main protein ribose-phosphate pyrophosphokinase from the Hakuna Genome, shares a homology with guanine phosphoribosyltransferase with an e score of 4e-10 according to HHPRED. The function and structure of this protein is to design compounds that would be effective inhibitors. "Almost all of the inhibitors available are analogues of the substrate or transition-state. The main drawback of these compounds is that there is poor differential inhibition among various HGPRTs. The reason maybe due to high structure similarity of HGPRTs from different species (especially the active site) even though there is only moderate sequence homology. The key residues in the active site are highly similar among HGPRTs (Table 1)."	complete CACAO 11622
involved_in	GO:0051289	protein homotetramerization	PMID:15990111^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00492	P		Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	PMID:9521733^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046100	hypoxanthine metabolic process	PMID:9824441^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046040	IMP metabolic process	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046038	GMP catabolic process	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045964	positive regulation of dopamine metabolic process	PMID:8643611^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043103	hypoxanthine salvage	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:8044844^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00492	F		Seeded From UniProt	complete
involved_in	GO:0006178	guanine salvage	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006166	purine ribonucleoside salvage	PMID:9824441^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006164	purine nucleotide biosynthetic process	PMID:9824441^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:6300847^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	PMID:19527031^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	PMID:6300847^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	PMID:9521733^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:10360366^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046100	hypoxanthine metabolic process	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96217 PANTHER:PTN000501530 RGD:2826 UniProtKB:F4IA25 UniProtKB:P00492	P		Seeded From UniProt	complete
involved_in	GO:0032264	IMP salvage	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG20098 PANTHER:PTN000501530	P		Seeded From UniProt	complete
involved_in	GO:0032263	GMP salvage	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG20098 PANTHER:PTN000501530	P		Seeded From UniProt	complete
involved_in	GO:0006178	guanine salvage	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96217 PANTHER:PTN000501530 UniProtKB:P00492 UniProtKB:Q9NRG1	P		Seeded From UniProt	complete
involved_in	GO:0006168	adenine salvage	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96217 PANTHER:PTN000501530	P		Seeded From UniProt	complete
involved_in	GO:0006166	purine ribonucleoside salvage	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96217 PANTHER:PTN000501530 UniProtKB:P00492 UniProtKB:Q8IJS1	P		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG20098 MGI:MGI:96217 PANTHER:PTN000501530 RGD:2826 UniProtKB:F4IA25 UniProtKB:P00492 UniProtKB:P9WHQ9 UniProtKB:Q8IJS1 UniProtKB:Q9NRG1 UniProtKB:Q9W719	F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG20098 PANTHER:PTN000501530 UniProtKB:P00492	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25416956^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00492	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0048813	dendrite morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0046651	lymphocyte proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0046100	hypoxanthine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0046083	adenine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0045964	positive regulation of dopamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	F		Seeded From UniProt	complete
involved_in	GO:0042417	dopamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0021954	central nervous system neuron development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0021895	cerebral cortex neuron differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0021756	striatum development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0007626	locomotory behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0007625	grooming behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0006178	guanine salvage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0006168	adenine salvage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0006166	purine ribonucleoside salvage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	C		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	F		Seeded From UniProt	complete
involved_in	GO:0001975	response to amphetamine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
involved_in	GO:0001913	T cell mediated cytotoxicity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00493 ensembl:ENSMUSP00000026723	P		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005904	F		Seeded From UniProt	complete
involved_in	GO:0006166	purine ribonucleoside salvage	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005904	P		Seeded From UniProt	complete
involved_in	GO:0009116	nucleoside metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000836	P		Seeded From UniProt	complete
enables	GO:0052657	guanine phosphoribosyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.4.2.8	F		Seeded From UniProt	complete
enables	GO:0004422	hypoxanthine phosphoribosyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.4.2.8	F		Seeded From UniProt	complete
involved_in	GO:0043101	purine-containing compound salvage	Reactome:R-HSA-74217	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-74215	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006166	purine ribonucleoside salvage	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0660	P		Seeded From UniProt	complete
enables	GO:0016757	transferase activity, transferring glycosyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0328	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0032264	IMP salvage	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00591	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Keough, DT et al. (2009) Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeutics. J. Med. Chem. 52 4391-9 PubMed GONUTS page
↑ Chen, Q et al. (2007) Crystal structure of Thermoanaerobacter tengcongensis hypoxanthine-guanine phosphoribosyl transferase L160I mutant--insights into inhibitor design. FEBS J. 274 4408-15 PubMed GONUTS page
↑ Keough, DT et al. (2005) The crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycle. J. Mol. Biol. 351 170-81 PubMed GONUTS page
↑ ^5.0 ^5.1 Xu, Y & Grubmeyer, C (1998) Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp 137 acts as a general acid/base. Biochemistry 37 4114-24 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Puig, JG et al. (1998) Purine metabolism in female heterozygotes for hypoxanthine-guanine phosphoribosyltransferase deficiency. Eur. J. Clin. Invest. 28 950-7 PubMed GONUTS page
↑ Wong, DF et al. (1996) Dopamine transporters are markedly reduced in Lesch-Nyhan disease in vivo. Proc. Natl. Acad. Sci. U.S.A. 93 5539-43 PubMed GONUTS page
↑ Eads, JC et al. (1994) The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78 325-34 PubMed GONUTS page
↑ ^9.0 ^9.1 Jolly, DJ et al. (1983) Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc. Natl. Acad. Sci. U.S.A. 80 477-81 PubMed GONUTS page
↑ Shi, W et al. (1999) The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat. Struct. Biol. 6 588-93 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 ^11.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page

[PMID:20458337-1] 1.0 ^1.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:19527031-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Keough, DT et al. (2009) Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeutics. J. Med. Chem. 52 4391-9 PubMed GONUTS page

[PMID:17662107-3] Chen, Q et al. (2007) Crystal structure of Thermoanaerobacter tengcongensis hypoxanthine-guanine phosphoribosyl transferase L160I mutant--insights into inhibitor design. FEBS J. 274 4408-15 PubMed GONUTS page

[PMID:15990111-4] Keough, DT et al. (2005) The crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycle. J. Mol. Biol. 351 170-81 PubMed GONUTS page

[PMID:9521733-5] 5.0 ^5.1 Xu, Y & Grubmeyer, C (1998) Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp 137 acts as a general acid/base. Biochemistry 37 4114-24 PubMed GONUTS page

[PMID:9824441-6] 6.0 ^6.1 ^6.2 Puig, JG et al. (1998) Purine metabolism in female heterozygotes for hypoxanthine-guanine phosphoribosyltransferase deficiency. Eur. J. Clin. Invest. 28 950-7 PubMed GONUTS page

[PMID:8643611-7] Wong, DF et al. (1996) Dopamine transporters are markedly reduced in Lesch-Nyhan disease in vivo. Proc. Natl. Acad. Sci. U.S.A. 93 5539-43 PubMed GONUTS page

[PMID:8044844-8] Eads, JC et al. (1994) The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78 325-34 PubMed GONUTS page

[PMID:6300847-9] 9.0 ^9.1 Jolly, DJ et al. (1983) Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc. Natl. Acad. Sci. U.S.A. 80 477-81 PubMed GONUTS page

[PMID:10360366-10] Shi, W et al. (1999) The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat. Struct. Biol. 6 588-93 PubMed GONUTS page

[PMID:21873635-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 ^11.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25416956-12] Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page

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HUMAN:HPRT

Contents

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References

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