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P27605 (HPRT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Hprt1
Synonyms:Hprt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

brain development

Inferred from expression pattern PubMed 6155447. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 2185659. Source: RGD

guanine salvage

Inferred from sequence or structural similarity. Source: UniProtKB

hypoxanthine metabolic process

Inferred from direct assay PubMed 6206848. Source: RGD

hypoxanthine salvage

Inferred from sequence or structural similarity. Source: UniProtKB

purine ribonucleoside salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

spermatogenesis

Inferred from expression pattern PubMed 12193390. Source: RGD

   Cellular_componentcytosol

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 6206848. Source: RGD

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_0000139591

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 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27605 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2683FC1444FE0B5E

FASTA21824,477
        10         20         30         40         50         60 
MSTLSPSVVI 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 YALDYNEHFR DLNHVCVISE SGKAKYKA 

« Hide

References

« Hide 'large scale' references
[1]"Rat hypoxanthine phosphoribosyltransferase cDNA cloning and sequence analysis."
Chiaverotti T.A., Battula N., Monnat R.J. Jr.
Genomics 11:1158-1160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat hypoxanthine phosphoribosyltransferase cDNA cloning and sequence analysis."
Chiaverotti T.A., Battula N., Monnat R.J. Jr.
Adv. Exp. Med. Biol. 309B:117-120(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The gene encoding hypoxanthine-guanine phosphoribosyltransferase as target for mutational analysis: PCR cloning and sequencing of the cDNA from the rat."
Jansen J.G., Vrieling H., van Zeeland A.A., Mohn G.R.
Mutat. Res. 266:105-116(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"DNA sequence flanking the protein coding regions of the rat Hprt gene."
Chen T., Mittelstaedt R.A., Heflich R.H.
Mutat. Res. 382:79-80(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Fischer 344.
Tissue: Spleen.
[5]"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: Thymus.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 35-45; 74-83; 92-101; 116-141; 157-166 AND 171-200, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[7]"Analysis of in vivo mutation in exon 8 of the rat hprt gene."
Mittelstaedt R.A., Heflich R.H.
Mutat. Res. 311:139-148(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-203.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63983 mRNA. Translation: AAA41350.1.
S79292 mRNA. Translation: AAB21288.1.
X62085 mRNA. Translation: CAA43997.1.
AF001282 expand/collapse EMBL AC list , AF001278, AF009655, AF009656, AF001279, AF001280, AF001281 Genomic DNA. Translation: AAB65640.1.
BC098629 mRNA. Translation: AAH98629.1.
U06049 Genomic DNA. Translation: AAA56887.1.
PIRS18140.
RefSeqNP_036715.1. NM_012583.2.
UniGeneRn.47.

3D structure databases

ProteinModelPortalP27605.
SMRP27605. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP27605. 2 interactions.
MINTMINT-4579300.

PTM databases

PhosphoSiteP27605.

2D gel databases

World-2DPAGE0004:P27605.

Proteomic databases

PaxDbP27605.
PRIDEP27605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000045153; ENSRNOP00000043388; ENSRNOG00000031367.
GeneID24465.
KEGGrno:24465.

Organism-specific databases

CTD3251.
RGD2826. Hprt1.

Phylogenomic databases

eggNOGCOG0634.
GeneTreeENSGT00390000017323.
HOGENOMHOG000236521.
HOVERGENHBG000242.
InParanoidP27605.
KOK00760.
OMAAREIMKG.
OrthoDBEOG7673CK.
PhylomeDBP27605.
TreeFamTF313367.

Enzyme and pathway databases

SABIO-RKP27605.
UniPathwayUPA00591; UER00648.

Gene expression databases

GenevestigatorP27605.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
InterProIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603395.
PROP27605.

Entry information

Entry nameHPRT_RAT
AccessionPrimary (citable) accession number: P27605
Secondary accession number(s): P70469, Q4KMC5, Q62926
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 112 of the entry and version 1 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