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P07741

- APT_HUMAN

UniProt

P07741 - APT_HUMAN

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Protein

Adenine phosphoribosyltransferase

Gene
APRT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.8 Publications
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 – 11Removed2 Publications
Chaini2 – 180179Adenine phosphoribosyltransferaseUniRule annotationPRO_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.

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. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 165 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

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