APT_HUMAN
ID APT_HUMAN Reviewed; 180 AA.
AC P07741; G5E9J2; Q3KP55; Q68DF9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000305};
DE Short=APRT;
DE EC=2.4.2.7 {ECO:0000269|PubMed:15196008};
GN Name=APRT {ECO:0000312|HGNC:HGNC:626};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3684585; DOI=10.1093/nar/15.21.9086;
RA Hidaka Y., Tarle S.A., Toole T.E.O., Kelley W.N., Palella T.D.;
RT "Nucleotide sequence of the human APRT gene.";
RL Nucleic Acids Res. 15:9086-9086(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3554238; DOI=10.1073/pnas.84.10.3349;
RA Broderick T.P., Schaff D.A., Bertino A.M., Dush M.K., Tischfield J.A.,
RA Stambrook P.J.;
RT "Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence
RT divergence and conservation of a nonrandom CpG dinucleotide arrangement.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3349-3353(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-121.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Astrocytoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-180.
RX PubMed=3531209; DOI=10.1016/s0021-9258(18)67074-7;
RA Wilson J.M., O'Toole T.E., Argos P., Shewach D.S., Daddona P.E.,
RA Kelley W.N.;
RT "Human adenine phosphoribosyltransferase. Complete amino acid sequence of
RT the erythrocyte enzyme.";
RL J. Biol. Chem. 261:13677-13683(1986).
RN [9]
RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-15; TYR-60; SER-66 AND THR-135, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-30 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=15196008; DOI=10.1021/bi0360758;
RA Silva M., Silva C.H., Iulek J., Thiemann O.H.;
RT "Three-dimensional structure of human adenine phosphoribosyltransferase and
RT its relation to DHA-urolithiasis.";
RL Biochemistry 43:7663-7671(2004).
RN [20]
RP VARIANT APRTD VAL-65.
RX PubMed=1746557;
RA Chen J., Sahota A., Laxdal T., Scrine M., Bowman S., Cui C.,
RA Stambrook P.J., Tischfield J.A.;
RT "Identification of a single missense mutation in the adenine
RT phosphoribosyltransferase (APRT) gene from five Icelandic patients and a
RT British patient.";
RL Am. J. Hum. Genet. 49:1306-1311(1991).
RN [21]
RP VARIANT APRTD PRO-110.
RX PubMed=7915931; DOI=10.1093/hmg/3.5.817;
RA Sahota A., Chen J., Boyadjiev S.A., Gault M.H., Tischfield J.A.;
RT "Missense mutation in the adenine phosphoribosyltransferase gene causing
RT 2,8-dihydroxyadenine urolithiasis.";
RL Hum. Mol. Genet. 3:817-818(1994).
RN [22]
RP VARIANT APRTD THR-136.
RX PubMed=3680503; DOI=10.1172/jci113219;
RA Hidaka Y., Palella T.D., O'Toole T.E., Tarle S.A., Kelley W.N.;
RT "Human adenine phosphoribosyltransferase. Identification of allelic
RT mutations at the nucleotide level as a cause of complete deficiency of the
RT enzyme.";
RL J. Clin. Invest. 80:1409-1415(1987).
RN [23]
RP VARIANTS APRTD THR-136 AND PHE-173 DEL.
RX PubMed=3343350; DOI=10.1172/jci113408;
RA Hidaka Y., Tarle S.A., Fujimori S., Kamatani N., Kelley W.N.;
RT "Human adenine phosphoribosyltransferase deficiency. Demonstration of a
RT single mutant allele common to the Japanese.";
RL J. Clin. Invest. 81:945-950(1988).
RN [24]
RP VARIANT APRTD THR-136.
RX PubMed=1353080; DOI=10.1172/jci115825;
RA Kamatani N., Hakoda M., Otsuka S., Yoshikawa H., Kashiwazaki S.;
RT "Only three mutations account for almost all defective alleles causing
RT adenine phosphoribosyltransferase deficiency in Japanese patients.";
RL J. Clin. Invest. 90:130-135(1992).
RN [25]
RP VARIANTS APRTD PHE-150 AND ARG-153.
RX PubMed=11243733; DOI=10.1006/mgme.2000.3142;
RA Deng L., Yang M., Fruend S., Wessel T., De Abreu R.A., Tischfield J.A.,
RA Sahota A.;
RT "2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual
RT adenine phosphoribosyltransferase activity in cell extracts but with
RT mutations in both copies of APRT.";
RL Mol. Genet. Metab. 72:260-264(2001).
RN [26]
RP VARIANTS APRTD MET-84 AND ASP-133.
RX PubMed=15571218; DOI=10.1081/ncn-200027393;
RA Taniguchi A., Tsuchida S., Kuno S., Mita M., Machida T., Ioritani N.,
RA Terai C., Yamanaka H., Kamatani N.;
RT "Identification of two novel mutations in adenine phosphoribosyltransferase
RT gene in patients with 2,8-dihydroxyadenine urolithiasis.";
RL Nucleosides Nucleotides Nucleic Acids 23:1141-1145(2004).
RN [27]
RP VARIANTS APRTD PRO-33 AND THR-136.
RX PubMed=21635362; DOI=10.1111/j.1651-2227.2011.02371.x;
RA Nozue H., Kamoda T., Saitoh H., Ichikawa K., Taniguchi A.;
RT "A Japanese boy with adenine phosphoribosyltransferase (APRT) deficiency
RT caused by compound heterozygosity including a novel missense mutation in
RT APRT gene.";
RL Acta Paediatr. 100:E285-E288(2011).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000269|PubMed:15196008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC Evidence={ECO:0000269|PubMed:15196008};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for 5-phospho-alpha-D-ribose 1-diphosphate
CC {ECO:0000269|PubMed:15196008};
CC KM=4 uM for adenine {ECO:0000269|PubMed:15196008};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000269|PubMed:15196008}.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P07741; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1047565, EBI-5235340;
CC P07741; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-1047565, EBI-948354;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07741-2; Sequence=VSP_045705;
CC -!- DISEASE: Adenine phosphoribosyltransferase deficiency (APRTD)
CC [MIM:614723]: An enzymatic deficiency that can lead to urolithiasis and
CC renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.
CC {ECO:0000269|PubMed:11243733, ECO:0000269|PubMed:1353080,
CC ECO:0000269|PubMed:15571218, ECO:0000269|PubMed:1746557,
CC ECO:0000269|PubMed:21635362, ECO:0000269|PubMed:3343350,
CC ECO:0000269|PubMed:3680503, ECO:0000269|PubMed:7915931}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/aprt/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Adenine phosphoribosyltransferase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase";
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DR EMBL; Y00486; CAA68543.1; -; Genomic_DNA.
DR EMBL; M16446; AAA51769.1; -; Genomic_DNA.
DR EMBL; CR749423; CAH18261.1; -; mRNA.
DR EMBL; AY306126; AAP45051.1; -; Genomic_DNA.
DR EMBL; AC092384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471184; EAW66761.1; -; Genomic_DNA.
DR EMBL; BC107151; AAI07152.1; -; mRNA.
DR EMBL; BM550173; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS32511.1; -. [P07741-1]
DR CCDS; CCDS45546.1; -. [P07741-2]
DR PIR; S06232; RTHUA.
DR RefSeq; NP_000476.1; NM_000485.2. [P07741-1]
DR RefSeq; NP_001025189.1; NM_001030018.1. [P07741-2]
DR PDB; 1ORE; X-ray; 2.10 A; A=1-180.
DR PDB; 1ZN7; X-ray; 1.83 A; A/B=1-180.
DR PDB; 1ZN8; X-ray; 1.76 A; A/B=2-180.
DR PDB; 1ZN9; X-ray; 2.05 A; A/B=1-180.
DR PDB; 4X44; X-ray; 2.05 A; A=1-180.
DR PDB; 4X45; X-ray; 1.75 A; A/B=1-180.
DR PDB; 6FCH; X-ray; 1.45 A; A/B=3-180.
DR PDB; 6FCI; X-ray; 1.94 A; A/B/C/D=2-180.
DR PDB; 6FCL; X-ray; 1.50 A; A/B=3-180.
DR PDB; 6FD4; X-ray; 1.50 A; A/B=3-180.
DR PDB; 6FD5; X-ray; 1.55 A; A/B=3-180.
DR PDB; 6FD6; X-ray; 1.80 A; A/B=3-180.
DR PDB; 6HGP; X-ray; 1.70 A; A/B=3-180.
DR PDB; 6HGQ; X-ray; 1.90 A; A/B/C/D=2-180.
DR PDB; 6HGR; X-ray; 1.52 A; A/B=3-180.
DR PDB; 6HGS; X-ray; 1.55 A; A/B=3-180.
DR PDBsum; 1ORE; -.
DR PDBsum; 1ZN7; -.
DR PDBsum; 1ZN8; -.
DR PDBsum; 1ZN9; -.
DR PDBsum; 4X44; -.
DR PDBsum; 4X45; -.
DR PDBsum; 6FCH; -.
DR PDBsum; 6FCI; -.
DR PDBsum; 6FCL; -.
DR PDBsum; 6FD4; -.
DR PDBsum; 6FD5; -.
DR PDBsum; 6FD6; -.
DR PDBsum; 6HGP; -.
DR PDBsum; 6HGQ; -.
DR PDBsum; 6HGR; -.
DR PDBsum; 6HGS; -.
DR AlphaFoldDB; P07741; -.
DR SMR; P07741; -.
DR BioGRID; 106849; 75.
DR IntAct; P07741; 12.
DR MINT; P07741; -.
DR STRING; 9606.ENSP00000367615; -.
DR ChEMBL; CHEMBL4105819; -.
DR DrugBank; DB01632; 5-O-phosphono-alpha-D-ribofuranosyl diphosphate.
DR DrugBank; DB03506; 5H-pyrrolo[3,2-d]pyrimidin-4-amine.
DR DrugBank; DB00173; Adenine.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB04272; Citric acid.
DR iPTMnet; P07741; -.
DR PhosphoSitePlus; P07741; -.
DR SwissPalm; P07741; -.
DR BioMuta; APRT; -.
DR DMDM; 114074; -.
DR SWISS-2DPAGE; P07741; -.
DR EPD; P07741; -.
DR jPOST; P07741; -.
DR MassIVE; P07741; -.
DR MaxQB; P07741; -.
DR PaxDb; P07741; -.
DR PeptideAtlas; P07741; -.
DR PRIDE; P07741; -.
DR ProteomicsDB; 33954; -.
DR ProteomicsDB; 52026; -. [P07741-1]
DR TopDownProteomics; P07741-1; -. [P07741-1]
DR TopDownProteomics; P07741-2; -. [P07741-2]
DR Antibodypedia; 17347; 353 antibodies from 32 providers.
DR DNASU; 353; -.
DR Ensembl; ENST00000378364.8; ENSP00000367615.3; ENSG00000198931.11. [P07741-1]
DR Ensembl; ENST00000426324.6; ENSP00000397007.2; ENSG00000198931.11. [P07741-2]
DR GeneID; 353; -.
DR KEGG; hsa:353; -.
DR MANE-Select; ENST00000378364.8; ENSP00000367615.3; NM_000485.3; NP_000476.1.
DR UCSC; uc002flv.4; human. [P07741-1]
DR CTD; 353; -.
DR DisGeNET; 353; -.
DR GeneCards; APRT; -.
DR GeneReviews; APRT; -.
DR HGNC; HGNC:626; APRT.
DR HPA; ENSG00000198931; Low tissue specificity.
DR MalaCards; APRT; -.
DR MIM; 102600; gene.
DR MIM; 614723; phenotype.
DR neXtProt; NX_P07741; -.
DR OpenTargets; ENSG00000198931; -.
DR Orphanet; 976; Adenine phosphoribosyltransferase deficiency.
DR PharmGKB; PA24914; -.
DR VEuPathDB; HostDB:ENSG00000198931; -.
DR eggNOG; KOG1712; Eukaryota.
DR GeneTree; ENSGT00390000017259; -.
DR HOGENOM; CLU_063339_3_2_1; -.
DR InParanoid; P07741; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; P07741; -.
DR TreeFam; TF300227; -.
DR PathwayCommons; P07741; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-74217; Purine salvage.
DR Reactome; R-HSA-9734195; Defective APRT disrupts adenine salvage.
DR SABIO-RK; P07741; -.
DR SignaLink; P07741; -.
DR UniPathway; UPA00588; UER00646.
DR BioGRID-ORCS; 353; 51 hits in 1080 CRISPR screens.
DR ChiTaRS; APRT; human.
DR EvolutionaryTrace; P07741; -.
DR GeneWiki; Adenine_phosphoribosyltransferase; -.
DR GenomeRNAi; 353; -.
DR Pharos; P07741; Tchem.
DR PRO; PR:P07741; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P07741; protein.
DR Bgee; ENSG00000198931; Expressed in skin of abdomen and 201 other tissues.
DR ExpressionAtlas; P07741; baseline and differential.
DR Genevisible; P07741; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IDA:MGI.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0032263; P:GMP salvage; IEA:Ensembl.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0032264; P:IMP salvage; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Glycosyltransferase;
KW Phosphoprotein; Purine salvage; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:3531209, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..180
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149504"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 134..180
FT /note="GTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE -> V
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045705"
FT VARIANT 33
FT /note="L -> P (in APRTD)"
FT /evidence="ECO:0000269|PubMed:21635362"
FT /id="VAR_069049"
FT VARIANT 65
FT /note="D -> V (in APRTD; Icelandic type;
FT dbSNP:rs104894506)"
FT /evidence="ECO:0000269|PubMed:1746557"
FT /id="VAR_006747"
FT VARIANT 84
FT /note="V -> M (in APRTD; dbSNP:rs200392753)"
FT /evidence="ECO:0000269|PubMed:15571218"
FT /id="VAR_069050"
FT VARIANT 110
FT /note="L -> P (in APRTD; Newfoundland type;
FT dbSNP:rs104894508)"
FT /evidence="ECO:0000269|PubMed:7915931"
FT /id="VAR_006748"
FT VARIANT 121
FT /note="Q -> R (in dbSNP:rs8191494)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019055"
FT VARIANT 133
FT /note="G -> D (in APRTD)"
FT /evidence="ECO:0000269|PubMed:15571218"
FT /id="VAR_069051"
FT VARIANT 136
FT /note="M -> T (in APRTD; Japanese type; allele APRT*J; most
FT common mutation; dbSNP:rs28999113)"
FT /evidence="ECO:0000269|PubMed:1353080,
FT ECO:0000269|PubMed:21635362, ECO:0000269|PubMed:3343350,
FT ECO:0000269|PubMed:3680503"
FT /id="VAR_006749"
FT VARIANT 150
FT /note="V -> F (in APRTD; dbSNP:rs281860266)"
FT /evidence="ECO:0000269|PubMed:11243733"
FT /id="VAR_022608"
FT VARIANT 153
FT /note="C -> R (in APRTD)"
FT /evidence="ECO:0000269|PubMed:11243733"
FT /id="VAR_022609"
FT VARIANT 173
FT /note="Missing (in APRTD)"
FT /evidence="ECO:0000269|PubMed:3343350"
FT /id="VAR_037575"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6FCL"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6FCH"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:6FCH"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6FCH"
SQ SEQUENCE 180 AA; 19608 MW; CDC7703337A6E453 CRC64;
MADSELQLVE QRIRSFPDFP TPGVVFRDIS PVLKDPASFR AAIGLLARHL KATHGGRIDY
IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTLWAS YSLEYGKAEL EIQKDALEPG
QRVVVVDDLL ATGGTMNAAC ELLGRLQAEV LECVSLVELT SLKGREKLAP VPFFSLLQYE
