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P00493

- HPRT_MOUSE

UniProt

P00493 - HPRT_MOUSE

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Protein
Hypoxanthine-guanine phosphoribosyltransferase
Gene
Hprt1, Hprt
Organism
Mus musculus (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: MGI
  3. identical protein binding Source: MGI
  4. magnesium ion binding Source: RefGenome
  5. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. GMP catabolic process Source: UniProtKB
  2. GMP salvage Source: RefGenome
  3. IMP metabolic process Source: UniProtKB
  4. IMP salvage Source: RefGenome
  5. adenine metabolic process Source: MGI
  6. adenine salvage Source: MGI
  7. central nervous system neuron development Source: MGI
  8. cerebral cortex neuron differentiation Source: MGI
  9. cytolysis Source: MGI
  10. dendrite morphogenesis Source: MGI
  11. dopamine metabolic process Source: MGI
  12. grooming behavior Source: MGI
  13. guanine salvage Source: MGI
  14. hypoxanthine metabolic process Source: MGI
  15. hypoxanthine salvage Source: UniProtKB
  16. locomotory behavior Source: MGI
  17. lymphocyte proliferation Source: MGI
  18. positive regulation of dopamine metabolic process Source: MGI
  19. protein homotetramerization Source: Ensembl
  20. purine ribonucleoside salvage Source: MGI
  21. response to amphetamine Source: MGI
  22. striatum development Source: MGI
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
Alternative name(s):
HPRT B
Gene namesi
Name:Hprt1
Synonyms:Hprt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:96217. Hprt.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: RefGenome
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_0000139588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP00493.
PaxDbiP00493.
PRIDEiP00493.

PTM databases

PhosphoSiteiP00493.

Expressioni

Gene expression databases

BgeeiP00493.
CleanExiMM_HPRT1.
GenevestigatoriP00493.

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

DIPiDIP-6034N.
MINTiMINT-217744.
STRINGi10090.ENSMUSP00000026723.

Structurei

3D structure databases

ProteinModelPortaliP00493.
SMRiP00493. Positions 5-218.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0634.
GeneTreeiENSGT00390000017323.
HOGENOMiHOG000236521.
HOVERGENiHBG000242.
InParanoidiP00493.
KOiK00760.
OMAiAREIMKG.
OrthoDBiEOG7673CK.
PhylomeDBiP00493.
TreeFamiTF313367.

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.

P00493-1 [UniParc]FASTAAdd to Basket

« Hide

MPTRSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA    50
RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI 100
RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV 150
KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR 200
DLNHVCVISE TGKAKYKA 218
Length:218
Mass (Da):24,570
Last modified:January 23, 2007 - v3
Checksum:i925CC0D4A6626E05
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011D → N in AAA96232. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00423 mRNA. Translation: AAA96232.1.
K01515
, 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.
CCDSiCCDS40972.1.
PIRiI49756. RTMSG.
RefSeqiNP_038584.2. NM_013556.2.
UniGeneiMm.299381.

Genome annotation databases

EnsembliENSMUST00000026723; ENSMUSP00000026723; ENSMUSG00000025630.
GeneIDi15452.
KEGGimmu:15452.
UCSCiuc009ter.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00423 mRNA. Translation: AAA96232.1 .
K01515
, 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 .
CCDSi CCDS40972.1.
PIRi I49756. RTMSG.
RefSeqi NP_038584.2. NM_013556.2.
UniGenei Mm.299381.

3D structure databases

ProteinModelPortali P00493.
SMRi P00493. Positions 5-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6034N.
MINTi MINT-217744.
STRINGi 10090.ENSMUSP00000026723.

PTM databases

PhosphoSitei P00493.

Proteomic databases

MaxQBi P00493.
PaxDbi P00493.
PRIDEi P00493.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026723 ; ENSMUSP00000026723 ; ENSMUSG00000025630 .
GeneIDi 15452.
KEGGi mmu:15452.
UCSCi uc009ter.1. mouse.

Organism-specific databases

CTDi 15452.
MGIi MGI:96217. Hprt.

Phylogenomic databases

eggNOGi COG0634.
GeneTreei ENSGT00390000017323.
HOGENOMi HOG000236521.
HOVERGENi HBG000242.
InParanoidi P00493.
KOi K00760.
OMAi AREIMKG.
OrthoDBi EOG7673CK.
PhylomeDBi P00493.
TreeFami TF313367.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00648 .

Miscellaneous databases

ChiTaRSi HPRT1. mouse.
NextBioi 288260.
PROi P00493.
SOURCEi Search...

Gene expression databases

Bgeei P00493.
CleanExi MM_HPRT1.
Genevestigatori P00493.

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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHPRT_MOUSE
AccessioniPrimary (citable) accession number: P00493
Secondary accession number(s): Q545Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 133 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

Complete proteome, Direct protein sequencing, Reference proteome

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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