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Q64531

- HPRT_MUSSP

UniProt

Q64531 - HPRT_MUSSP

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Protein
Hypoxanthine-guanine phosphoribosyltransferase
Gene
Hprt1, Hprt
Organism
Mus spretus (Western Mediterranean mouse) (Algerian mouse)
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 By similarity.

Catalytic activityi

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactori

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.

Pathwayi

Sites

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

Regions

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

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 homodimerization activity Source: UniProtKB

GO - Biological processi

  1. GMP catabolic process Source: UniProtKB
  2. IMP metabolic process Source: UniProtKB
  3. IMP salvage Source: UniProtKB-UniPathway
  4. guanine salvage Source: UniProtKB
  5. hypoxanthine metabolic process Source: UniProtKB
  6. hypoxanthine salvage Source: UniProtKB
  7. positive regulation of dopamine metabolic process Source: UniProtKB
  8. protein homotetramerization Source: UniProtKB
  9. purine nucleotide biosynthetic process Source: UniProtKB
  10. purine ribonucleoside salvage Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00591; UER00648.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
Short name:
HGPRT
Short name:
HGPRTase
Short name:
HPRT A
Gene namesi
Name:Hprt1
Synonyms:Hprt
OrganismiMus spretus (Western Mediterranean mouse) (Algerian mouse)
Taxonomic identifieri10096 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Organism-specific databases

MGIiMGI:96217. Hprt1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – ›214›213Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine Inferred
Modified residuei103 – 1031N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ64531.
SMRiQ64531. Positions 5-214.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000242.

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: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64531-1 [UniParc]FASTAAdd to Basket

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MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG LIMDRTERLA    50
RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI 100
RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV 150
KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR 200
DLNHVCVISE TGKA 214
Length:214
Mass (Da):24,082
Last modified:January 23, 2007 - v3
Checksum:i986078ACAF2688C3
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei214 – 2141

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20011 mRNA. Translation: AAA96234.1.
PIRiI49758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20011 mRNA. Translation: AAA96234.1 .
PIRi I49758.

3D structure databases

ProteinModelPortali Q64531.
SMRi Q64531. Positions 5-214.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:96217. Hprt1.

Phylogenomic databases

HOVERGENi HBG000242.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00648 .

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

  1. "Altered turnover of allelic variants of hypoxanthine phosphoribosyltransferase is associated with N-terminal amino acid sequence variation."
    Johnson G.G., Kronert W.A., Bernstein S.I., Chapman V.M., Smith K.D.
    J. Biol. Chem. 263:9079-9082(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.

Entry informationi

Entry nameiHPRT_MUSSP
AccessioniPrimary (citable) accession number: Q64531
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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