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P00493 (HPRT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
Alternative name(s):
HPRT B
Gene names
Name:Hprt1
Synonyms:Hprt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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 processPurine salvage
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGMP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

GMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

IMP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

IMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenine metabolic process

Inferred from mutant phenotype PubMed 8894695. Source: MGI

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 metabolic process

Inferred from mutant phenotype PubMed 10037486PubMed 3029599. Source: MGI

hypoxanthine salvage

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from mutant phenotype PubMed 12812988. Source: MGI

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: Ensembl

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_componentcytoplasm

Inferred from direct assay PubMed 8193672. Source: MGI

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionguanine 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

identical protein binding

Inferred from physical interaction PubMed 11591653. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 218217Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139588

Regions

Nucleotide binding134 – 1429GMP By similarity
Nucleotide binding186 – 1883GMP By similarity

Sites

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

Amino acid modifications

Modified residue1031N6-acetyllysine Ref.6

Experimental info

Sequence conflict2011D → N in AAA96232. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00493 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 925CC0D4A6626E05

FASTA21824,570
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00423 mRNA. Translation: AAA96232.1.
K01515 expand/collapse EMBL AC list , 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.
PIRRTMSG. I49756.
RefSeqNP_038584.2. NM_013556.2.
UniGeneMm.299381.

3D structure databases

ProteinModelPortalP00493.
SMRP00493. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6034N.
MINTMINT-217744.
STRING10090.ENSMUSP00000026723.

PTM databases

PhosphoSiteP00493.

Proteomic databases

PaxDbP00493.
PRIDEP00493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026723; ENSMUSP00000026723; ENSMUSG00000025630.
GeneID15452.
KEGGmmu:15452.
UCSCuc009ter.1. mouse.

Organism-specific databases

CTD15452.
MGIMGI:96217. Hprt.

Phylogenomic databases

eggNOGCOG0634.
GeneTreeENSGT00390000017323.
HOGENOMHOG000236521.
HOVERGENHBG000242.
InParanoidP00493.
KOK00760.
OMALIMDSRT.
OrthoDBEOG7673CK.
PhylomeDBP00493.
TreeFamTF313367.

Enzyme and pathway databases

UniPathwayUPA00591; UER00648.

Gene expression databases

BgeeP00493.
CleanExMM_HPRT1.
GenevestigatorP00493.

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. mouse.
NextBio288260.
PROP00493.
SOURCESearch...

Entry information

Entry nameHPRT_MOUSE
AccessionPrimary (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 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot