P00493 (HPRT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hypoxanthine-guanine phosphoribosyltransferase
Short name=HGPRT
Short name=HGPRTase
EC=2.4.2.8

Alternative name(s):
HPRT B

Gene names

Name:	Hprt1
Synonyms:	Hprt

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.
Cofactor	Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein By similarity.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GMP catabolic process Inferred from sequence or structural similarity. Source: UniProtKB GMP salvage Inferred from Biological aspect of Ancestor. Source: RefGenome IMP salvage Inferred from Biological aspect of Ancestor. Source: RefGenome adenine salvage Inferred from mutant phenotype PubMed 10037486. Source: MGI central nervous system neuron development Inferred from mutant phenotype PubMed 9886073. Source: MGI cerebral cortex neuron differentiation Inferred from mutant phenotype PubMed 11297820. Source: MGI cytolysis Inferred from mutant phenotype PubMed 12944494. Source: MGI dendrite morphogenesis Inferred from mutant phenotype PubMed 11297820. Source: MGI dopamine metabolic process Inferred from mutant phenotype PubMed 1432691PubMed 9886073. Source: MGI grooming behavior Inferred from genetic interaction PubMed 8485579. Source: MGI guanine salvage Inferred from mutant phenotype PubMed 10037486. Source: MGI hypoxanthine salvage Inferred from sequence or structural similarity. Source: UniProtKB lymphocyte proliferation Inferred from mutant phenotype PubMed 12944494. Source: MGI positive regulation of dopamine metabolic process Inferred from mutant phenotype PubMed 7509865. Source: MGI protein homotetramerization Inferred from electronic annotation. Source: Compara purine ribonucleoside salvage Inferred from mutant phenotype PubMed 10037486PubMed 12944494PubMed 8485579PubMed 8492116. Source: MGI response to amphetamine Inferred from mutant phenotype PubMed 1432691PubMed 1777100. Source: MGI striatum development Inferred from mutant phenotype PubMed 9886073. Source: MGI
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	guanine phosphoribosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB hypoxanthine phosphoribosyltransferase activity Inferred from direct assay PubMed 1235912PubMed 12944494PubMed 198184PubMed 204065PubMed 2890215PubMed 2906327PubMed 291939PubMed 3243423PubMed 540025PubMed 6251472Ref.2PubMed 6852525PubMed 8492116PubMed 8878108PubMed 943046. Source: MGI magnesium ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 218	217	Hypoxanthine-guanine phosphoribosyltransferase		PRO_0000139588
Regions
	Nucleotide binding	134 – 142	9	GMP By similarity
	Nucleotide binding	186 – 188	3	GMP By similarity
Sites
	Active site	138	1	Proton acceptor By similarity
	Metal binding	194	1	Magnesium By similarity
	Binding site	69	1	GMP By similarity
	Binding site	166	1	GMP By similarity
	Binding site	194	1	GMP; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	201	1	D → N in AAA96232. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P00493 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 925CC0D4A6626E05	FASTA	218	24,570
	10 20 30 40 50 60 MPTRSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH 70 80 90 100 110 120 HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD 130 140 150 160 170 180 DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG 190 200 210 FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese hamster: construction and sequence analysis of cDNA recombinants." Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C. Nucleic Acids Res. 10:6763-6775(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure, expression, and mutation of the hypoxanthine phosphoribosyltransferase gene." Melton D.W., Konecki D.S., Brennand J., Caskey C.T. Proc. Natl. Acad. Sci. U.S.A. 81:2147-2151(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Myeloma.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Heart and Thymus.
[4]	"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]. Strain: C57BL/6J. Tissue: Embryo.
[5]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 74-83 AND 171-200, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J00423 mRNA. Translation: AAA96232.1. K01515 , K01507, K01508, K01509, K01510, K01511, K01512, K01513, K01514 Genomic DNA. Translation: AAA96271.1. AK002286 mRNA. Translation: BAB21989.1. AK088114 mRNA. Translation: BAC40153.1. AK146626 mRNA. Translation: BAE27315.1. BC083145 mRNA. Translation: AAH83145.1.
IPI	IPI00284806.
PIR	RTMSG. I49756.
RefSeq	NP_038584.2. NM_013556.2.
UniGene	Mm.299381.
3D structure databases
ProteinModelPortal	P00493.
SMR	P00493. Positions 5-218.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6034N.
MINT	MINT-217744.
STRING	10090.ENSMUSP00000026723.
PTM databases
PhosphoSite	P00493.
Proteomic databases
PaxDb	P00493.
PRIDE	P00493.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026723; ENSMUSP00000026723; ENSMUSG00000025630.
GeneID	15452.
KEGG	mmu:15452.
Organism-specific databases
CTD	15452.
MGI	MGI:96217. Hprt.
Phylogenomic databases
eggNOG	COG0634.
GeneTree	ENSGT00390000017323.
HOGENOM	HOG000236521.
HOVERGEN	HBG000242.
InParanoid	P00493.
KO	K00760.
OrthoDB	EOG4H72CM.
Enzyme and pathway databases
UniPathway	UPA00591; UER00648.
Gene expression databases
ArrayExpress	P00493.
Bgee	P00493.
CleanEx	MM_HPRT1.
Genevestigator	P00493.
GermOnline	ENSMUSG00000025630. Mus musculus.
Family and domain databases
InterPro	IPR005904. Hxn_phspho_trans. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01203. HGPRTase. 1 hit.
PROSITE	PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HPRT1. mouse.
NextBio	288260.
SOURCE	Search...

Entry information

Entry name

HPRT_MOUSE

Accession

Primary (citable) accession number: P00493
Secondary accession number(s): Q545Y2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program