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P07741

- APT_HUMAN

UniProt

P07741 - APT_HUMAN

Protein

Adenine phosphoribosyltransferase

Gene

APRT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.

    Catalytic activityi

    AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.

    Pathwayi

    GO - Molecular functioni

    1. adenine binding Source: Ensembl
    2. adenine phosphoribosyltransferase activity Source: Reactome
    3. AMP binding Source: MGI

    GO - Biological processi

    1. adenine salvage Source: Ensembl
    2. AMP salvage Source: UniProtKB-UniPathway
    3. cellular response to insulin stimulus Source: Ensembl
    4. grooming behavior Source: Ensembl
    5. lactation Source: Ensembl
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. purine-containing compound salvage Source: Reactome
    8. purine nucleobase metabolic process Source: Reactome
    9. purine ribonucleoside salvage Source: UniProtKB-KW
    10. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    BRENDAi2.4.2.7. 2681.
    ReactomeiREACT_1923. Purine salvage.
    SABIO-RKP07741.
    UniPathwayiUPA00588; UER00646.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenine phosphoribosyltransferase (EC:2.4.2.7)
    Short name:
    APRT
    Gene namesi
    Name:APRT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:626. APRT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Adenine phosphoribosyltransferase deficiency (APRTD) [MIM:614723]: An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331L → P in APRTD. 1 Publication
    VAR_069049
    Natural varianti65 – 651D → V in APRTD; Icelandic type. 1 Publication
    VAR_006747
    Natural varianti84 – 841V → M in APRTD. 1 Publication
    Corresponds to variant rs200392753 [ dbSNP | Ensembl ].
    VAR_069050
    Natural varianti110 – 1101L → P in APRTD; Newfoundland type. 1 Publication
    VAR_006748
    Natural varianti133 – 1331G → D in APRTD. 1 Publication
    VAR_069051
    Natural varianti136 – 1361M → T in APRTD; Japanese type; allele APRT*J; most common mutation. 4 Publications
    Corresponds to variant rs28999113 [ dbSNP | Ensembl ].
    VAR_006749
    Natural varianti150 – 1501V → F in APRTD. 1 Publication
    VAR_022608
    Natural varianti153 – 1531C → R in APRTD. 1 Publication
    VAR_022609
    Natural varianti173 – 1731Missing in APRTD. 1 Publication
    VAR_037575

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614723. phenotype.
    Orphaneti976. Adenine phosphoribosyltransferase deficiency.
    PharmGKBiPA24914.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 180179Adenine phosphoribosyltransferasePRO_0000149504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei15 – 151Phosphoserine1 Publication
    Modified residuei60 – 601Phosphotyrosine1 Publication
    Modified residuei66 – 661Phosphoserine1 Publication
    Modified residuei114 – 1141N6-acetyllysine1 Publication
    Modified residuei135 – 1351Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP07741.
    PaxDbiP07741.
    PRIDEiP07741.

    2D gel databases

    SWISS-2DPAGEP07741.

    PTM databases

    PhosphoSiteiP07741.

    Expressioni

    Gene expression databases

    ArrayExpressiP07741.
    BgeeiP07741.
    CleanExiHS_APRT.
    GenevestigatoriP07741.

    Organism-specific databases

    HPAiHPA026681.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi106849. 14 interactions.
    IntActiP07741. 2 interactions.
    MINTiMINT-4999823.
    STRINGi9606.ENSP00000367615.

    Structurei

    Secondary structure

    1
    180
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Beta strandi14 – 174
    Beta strandi19 – 213
    Beta strandi25 – 284
    Helixi30 – 345
    Helixi36 – 5419
    Beta strandi60 – 645
    Turni65 – 673
    Helixi68 – 7912
    Beta strandi82 – 887
    Beta strandi94 – 10310
    Beta strandi106 – 1138
    Beta strandi122 – 13312
    Helixi134 – 14512
    Beta strandi149 – 15911
    Helixi160 – 1623
    Helixi164 – 1685
    Beta strandi173 – 1797

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OPUmodel-A1-180[»]
    1OREX-ray2.10A1-180[»]
    1ZN7X-ray1.83A/B1-180[»]
    1ZN8X-ray1.76A/B2-180[»]
    1ZN9X-ray2.05A/B1-180[»]
    ProteinModelPortaliP07741.
    SMRiP07741. Positions 2-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07741.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0503.
    HOGENOMiHOG000036776.
    HOVERGENiHBG003144.
    InParanoidiP07741.
    KOiK00759.
    OMAiTTYSERD.
    OrthoDBiEOG7FFMT9.
    PhylomeDBiP07741.
    TreeFamiTF300227.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    HAMAPiMF_00004. Aden_phosphoribosyltr.
    InterProiIPR005764. Ade_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01090. apt. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07741-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADSELQLVE QRIRSFPDFP TPGVVFRDIS PVLKDPASFR AAIGLLARHL    50
    KATHGGRIDY IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTLWAS 100
    YSLEYGKAEL EIQKDALEPG QRVVVVDDLL ATGGTMNAAC ELLGRLQAEV 150
    LECVSLVELT SLKGREKLAP VPFFSLLQYE 180
    Length:180
    Mass (Da):19,608
    Last modified:January 23, 2007 - v2
    Checksum:iCDC7703337A6E453
    GO
    Isoform 2 (identifier: P07741-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-180: GTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE → V

    Note: No experimental confirmation available.

    Show »
    Length:134
    Mass (Da):14,557
    Checksum:i404EC4ACAE4C29DE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331L → P in APRTD. 1 Publication
    VAR_069049
    Natural varianti65 – 651D → V in APRTD; Icelandic type. 1 Publication
    VAR_006747
    Natural varianti84 – 841V → M in APRTD. 1 Publication
    Corresponds to variant rs200392753 [ dbSNP | Ensembl ].
    VAR_069050
    Natural varianti110 – 1101L → P in APRTD; Newfoundland type. 1 Publication
    VAR_006748
    Natural varianti121 – 1211Q → R.1 Publication
    Corresponds to variant rs8191494 [ dbSNP | Ensembl ].
    VAR_019055
    Natural varianti133 – 1331G → D in APRTD. 1 Publication
    VAR_069051
    Natural varianti136 – 1361M → T in APRTD; Japanese type; allele APRT*J; most common mutation. 4 Publications
    Corresponds to variant rs28999113 [ dbSNP | Ensembl ].
    VAR_006749
    Natural varianti150 – 1501V → F in APRTD. 1 Publication
    VAR_022608
    Natural varianti153 – 1531C → R in APRTD. 1 Publication
    VAR_022609
    Natural varianti173 – 1731Missing in APRTD. 1 Publication
    VAR_037575

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 18047GTMNA…LLQYE → V in isoform 2. 1 PublicationVSP_045705Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00486 Genomic DNA. Translation: CAA68543.1.
    M16446 Genomic DNA. Translation: AAA51769.1.
    CR749423 mRNA. Translation: CAH18261.1.
    AY306126 Genomic DNA. Translation: AAP45051.1.
    AC092384 Genomic DNA. No translation available.
    CH471184 Genomic DNA. Translation: EAW66761.1.
    BC107151 mRNA. Translation: AAI07152.1.
    BM550173 mRNA. No translation available.
    CCDSiCCDS32511.1. [P07741-1]
    CCDS45546.1. [P07741-2]
    PIRiS06232. RTHUA.
    RefSeqiNP_000476.1. NM_000485.2. [P07741-1]
    NP_001025189.1. NM_001030018.1. [P07741-2]
    UniGeneiHs.28914.

    Genome annotation databases

    EnsembliENST00000378364; ENSP00000367615; ENSG00000198931. [P07741-1]
    ENST00000426324; ENSP00000397007; ENSG00000198931. [P07741-2]
    GeneIDi353.
    KEGGihsa:353.
    UCSCiuc002flv.3. human. [P07741-1]
    uc002flw.3. human.

    Polymorphism databases

    DMDMi114074.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Adenine phosphoribosyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00486 Genomic DNA. Translation: CAA68543.1 .
    M16446 Genomic DNA. Translation: AAA51769.1 .
    CR749423 mRNA. Translation: CAH18261.1 .
    AY306126 Genomic DNA. Translation: AAP45051.1 .
    AC092384 Genomic DNA. No translation available.
    CH471184 Genomic DNA. Translation: EAW66761.1 .
    BC107151 mRNA. Translation: AAI07152.1 .
    BM550173 mRNA. No translation available.
    CCDSi CCDS32511.1. [P07741-1 ]
    CCDS45546.1. [P07741-2 ]
    PIRi S06232. RTHUA.
    RefSeqi NP_000476.1. NM_000485.2. [P07741-1 ]
    NP_001025189.1. NM_001030018.1. [P07741-2 ]
    UniGenei Hs.28914.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OPU model - A 1-180 [» ]
    1ORE X-ray 2.10 A 1-180 [» ]
    1ZN7 X-ray 1.83 A/B 1-180 [» ]
    1ZN8 X-ray 1.76 A/B 2-180 [» ]
    1ZN9 X-ray 2.05 A/B 1-180 [» ]
    ProteinModelPortali P07741.
    SMRi P07741. Positions 2-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106849. 14 interactions.
    IntActi P07741. 2 interactions.
    MINTi MINT-4999823.
    STRINGi 9606.ENSP00000367615.

    Chemistry

    DrugBanki DB00173. Adenine.
    DB00131. Adenosine monophosphate.

    PTM databases

    PhosphoSitei P07741.

    Polymorphism databases

    DMDMi 114074.

    2D gel databases

    SWISS-2DPAGE P07741.

    Proteomic databases

    MaxQBi P07741.
    PaxDbi P07741.
    PRIDEi P07741.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378364 ; ENSP00000367615 ; ENSG00000198931 . [P07741-1 ]
    ENST00000426324 ; ENSP00000397007 ; ENSG00000198931 . [P07741-2 ]
    GeneIDi 353.
    KEGGi hsa:353.
    UCSCi uc002flv.3. human. [P07741-1 ]
    uc002flw.3. human.

    Organism-specific databases

    CTDi 353.
    GeneCardsi GC16M088875.
    GeneReviewsi APRT.
    HGNCi HGNC:626. APRT.
    HPAi HPA026681.
    MIMi 102600. gene.
    614723. phenotype.
    neXtProti NX_P07741.
    Orphaneti 976. Adenine phosphoribosyltransferase deficiency.
    PharmGKBi PA24914.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0503.
    HOGENOMi HOG000036776.
    HOVERGENi HBG003144.
    InParanoidi P07741.
    KOi K00759.
    OMAi TTYSERD.
    OrthoDBi EOG7FFMT9.
    PhylomeDBi P07741.
    TreeFami TF300227.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00646 .
    BRENDAi 2.4.2.7. 2681.
    Reactomei REACT_1923. Purine salvage.
    SABIO-RK P07741.

    Miscellaneous databases

    EvolutionaryTracei P07741.
    GeneWikii Adenine_phosphoribosyltransferase.
    GenomeRNAii 353.
    NextBioi 1453.
    PROi P07741.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07741.
    Bgeei P07741.
    CleanExi HS_APRT.
    Genevestigatori P07741.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    HAMAPi MF_00004. Aden_phosphoribosyltr.
    InterProi IPR005764. Ade_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01090. apt. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    2. "Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement."
      Broderick T.P., Schaff D.A., Bertino A.M., Dush M.K., Tischfield J.A., Stambrook P.J.
      Proc. Natl. Acad. Sci. U.S.A. 84:3349-3353(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterine endothelium.
    4. NIEHS SNPs program
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-121.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Astrocytoma.
    8. "Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme."
      Wilson J.M., O'Toole T.E., Argos P., Shewach D.S., Daddona P.E., Kelley W.N.
      J. Biol. Chem. 261:13677-13683(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-180.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-15; TYR-60; SER-66 AND THR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis."
      Silva M., Silva C.H., Iulek J., Thiemann O.H.
      Biochemistry 43:7663-7671(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    17. "Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient."
      Chen J., Sahota A., Laxdal T., Scrine M., Bowman S., Cui C., Stambrook P.J., Tischfield J.A.
      Am. J. Hum. Genet. 49:1306-1311(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APRTD VAL-65.
    18. "Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis."
      Sahota A., Chen J., Boyadjiev S.A., Gault M.H., Tischfield J.A.
      Hum. Mol. Genet. 3:817-818(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APRTD PRO-110.
    19. "Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme."
      Hidaka Y., Palella T.D., O'Toole T.E., Tarle S.A., Kelley W.N.
      J. Clin. Invest. 80:1409-1415(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APRTD THR-136.
    20. "Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese."
      Hidaka Y., Tarle S.A., Fujimori S., Kamatani N., Kelley W.N.
      J. Clin. Invest. 81:945-950(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS APRTD THR-136 AND PHE-173 DEL.
    21. "Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients."
      Kamatani N., Hakoda M., Otsuka S., Yoshikawa H., Kashiwazaki S.
      J. Clin. Invest. 90:130-135(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APRTD THR-136.
    22. "2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT."
      Deng L., Yang M., Fruend S., Wessel T., De Abreu R.A., Tischfield J.A., Sahota A.
      Mol. Genet. Metab. 72:260-264(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS APRTD PHE-150 AND ARG-153.
    23. "Identification of two novel mutations in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis."
      Taniguchi A., Tsuchida S., Kuno S., Mita M., Machida T., Ioritani N., Terai C., Yamanaka H., Kamatani N.
      Nucleosides Nucleotides Nucleic Acids 23:1141-1145(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS APRTD MET-84 AND ASP-133.
    24. "A Japanese boy with adenine phosphoribosyltransferase (APRT) deficiency caused by compound heterozygosity including a novel missense mutation in APRT gene."
      Nozue H., Kamoda T., Saitoh H., Ichikawa K., Taniguchi A.
      Acta Paediatr. 100:E285-E288(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS APRTD PRO-33 AND THR-136.

    Entry informationi

    Entry nameiAPT_HUMAN
    AccessioniPrimary (citable) accession number: P07741
    Secondary accession number(s): G5E9J2, Q3KP55, Q68DF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 166 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3