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P00494

- HPRT_CRIGR

UniProt

P00494 - HPRT_CRIGR

Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

HPRT1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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.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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691GMPBy similarity
    Active sitei138 – 1381Proton acceptorBy similarity
    Binding sitei166 – 1661GMPBy similarity
    Metal bindingi194 – 1941MagnesiumBy similarity
    Binding sitei194 – 1941GMP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi134 – 1429GMPBy similarity
    Nucleotide bindingi186 – 1883GMPBy 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. guanine salvage Source: UniProtKB
    3. hypoxanthine metabolic process Source: UniProtKB
    4. hypoxanthine salvage Source: UniProtKB
    5. IMP metabolic process Source: UniProtKB
    6. IMP salvage Source: UniProtKB-UniPathway
    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

    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
    Gene namesi
    Name:HPRT1
    Synonyms:HPRT
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 218217Hypoxanthine-guanine phosphoribosyltransferasePRO_0000139584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei103 – 1031N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP00494.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP00494.
    SMRiP00494. Positions 5-218.
    ModBaseiSearch...
    MobiDBiSearch...

    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: Complete.

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

    P00494-1 [UniParc]FASTAAdd to Basket

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    MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG VIMDRTERLA    50
    RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI 100
    RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV 150
    KRYNLKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR 200
    DLNHICVISE TGKAKYKA 218
    Length:218
    Mass (Da):24,644
    Last modified:January 23, 2007 - v2
    Checksum:i21DA6A26D92B7511
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321L → M in AAP13884. (PubMed:1383700)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00060 mRNA. Translation: AAA36990.1.
    X53073
    , X53074, X53075, X53076, X53077, X53078, X53079, X53080 Genomic DNA. Translation: CAA37247.1.
    S46270 Genomic DNA. Translation: AAP13884.1.
    PIRiS14402. RTHYG.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00060 mRNA. Translation: AAA36990.1 .
    X53073
    , X53074 , X53075 , X53076 , X53077 , X53078 , X53079 , X53080 Genomic DNA. Translation: CAA37247.1 .
    S46270 Genomic DNA. Translation: AAP13884.1 .
    PIRi S14402. RTHYG.

    3D structure databases

    ProteinModelPortali P00494.
    SMRi P00494. Positions 5-218.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P00494.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "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. "The Chinese hamster HPRT gene: restriction map, sequence analysis, and multiplex PCR deletion screen."
      Rossiter B.J.F., Fuscoe J.C., Muzny D.M., Fox M., Caskey C.T.
      Genomics 9:247-256(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Analysis of X-ray-induced HPRT mutations in CHO cells: insertion and deletions."
      Fuscoe J.C., Zimmerman L.J., Fekete A., Setzer R.W., Rossiter B.J.
      Mutat. Res. 269:171-183(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-42.

    Entry informationi

    Entry nameiHPRT_CRIGR
    AccessioniPrimary (citable) accession number: P00494
    Secondary accession number(s): Q80XX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The cell lines from which this sequence was cloned are revertants from mutants with no detectable enzyme activity. The phenotypic reversions are the result of overproduction of variant enzymes because of gene amplification. This variant sequence is expected to be very similar to the wild-type.

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3