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P00494

- HPRT_CRIGR

UniProt

P00494 - HPRT_CRIGR

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Protein
Hypoxanthine-guanine phosphoribosyltransferase
Gene
HPRT1, HPRT
Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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
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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 218217Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139584Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00494.

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP00494.
SMRiP00494. Positions 5-218.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321L → M in AAP13884. 1 Publication

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: June 11, 2014
This is version 86 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

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