MTAP_HUMAN
ID MTAP_HUMAN Reviewed; 283 AA.
AC Q13126; I2G7M5; I2G7M6; I2G7M7; I2G7M8; I2G7M9; I2G7N0; Q5T3P3; Q9H010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_03155};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAPase {ECO:0000255|HAMAP-Rule:MF_03155};
GN Name=MTAP {ECO:0000255|HAMAP-Rule:MF_03155}; Synonyms=MSAP;
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 [MRNA], AND VARIANT ILE-56.
RC TISSUE=Epidermis;
RX PubMed=7604019; DOI=10.1073/pnas.92.14.6489;
RA Olopade O.I., Pomykala H.M., Hagos F., Sveen L.W., Espinosa R. III,
RA Dreyling M.H., Gursky S., Stadler W.M., le Beau M.M., Bohlander S.K.;
RT "Construction of a 2.8-megabase yeast artificial chromosome contig and
RT cloning of the human methylthioadenosine phosphorylase gene from the tumor
RT suppressor region on 9p21.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6489-6493(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Placenta;
RX PubMed=8650244; DOI=10.1073/pnas.93.12.6203;
RA Nobori T., Takabayashi K., Tran P., Orvis L., Batova A., Yu A.L.,
RA Carson D.A.;
RT "Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic
RT enzyme deficient in multiple different cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6203-6208(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7), AND INVOLVEMENT
RP IN DMSMFH.
RX PubMed=22464254; DOI=10.1016/j.ajhg.2012.02.024;
RA Camacho-Vanegas O., Camacho S.C., Till J., Miranda-Lorenzo I., Terzo E.,
RA Ramirez M.C., Schramm V., Cordovano G., Watts G., Mehta S., Kimonis V.,
RA Hoch B., Philibert K.D., Raabe C.A., Bishop D.F., Glucksman M.J.,
RA Martignetti J.A.;
RT "Primate genome gain and loss: a bone dysplasia, muscular dystrophy, and
RT bone cancer syndrome resulting from mutated retroviral-derived MTAP
RT transcripts.";
RL Am. J. Hum. Genet. 90:614-627(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-56.
RC TISSUE=Colon;
RA Li Q., Cao W.-X., Zhang Y., Shi M.-M., Liu B.-Y., Zhu Z.-G., Lin Y.-Z.;
RT "Identification of human methylthioadenosine phosphorylase (MTAP) mRNA
RT mutation in colon cancer cell line COLO 205.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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], AND VARIANT ILE-56.
RC TISSUE=Brain;
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=3091600; DOI=10.1016/s0021-9258(18)67242-4;
RA Della Ragione F., Carteni-Farina M., Gragnaniello V., Schettino M.I.,
RA Zappia V.;
RT "Purification and characterization of 5'-deoxy-5'-methylthioadenosine
RT phosphorylase from human placenta.";
RL J. Biol. Chem. 261:12324-12329(1986).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=8687427; DOI=10.1006/bbrc.1996.0926;
RA Ragione F.D., Takabayashi K., Mastropietro S., Mercurio C., Oliva A.,
RA Russo G.L., Pietra V.D., Borriello A., Nobori T., Carson D.A., Zappia V.;
RT "Purification and characterization of recombinant human 5'-
RT methylthioadenosine phosphorylase: definite identification of coding
RT cDNA.";
RL Biochem. Biophys. Res. Commun. 223:514-519(1996).
RN [10]
RP INVOLVEMENT IN OSTEOSARCOMA.
RX PubMed=11895909;
RA Garcia-Castellano J.M., Villanueva A., Healey J.H., Sowers R.,
RA Cordon-Cardo C., Huvos A., Bertino J.R., Meyers P., Gorlick R.;
RT "Methylthioadenosine phosphorylase gene deletions are common in
RT osteosarcoma.";
RL Clin. Cancer Res. 8:782-787(2002).
RN [11]
RP INVOLVEMENT IN OSTEOSARCOMA.
RX PubMed=17912432;
RA Miyazaki S., Nishioka J., Shiraishi T., Matsumine A., Uchida A., Nobori T.;
RT "Methylthioadenosine phosphorylase deficiency in Japanese osteosarcoma
RT patients.";
RL Int. J. Oncol. 31:1069-1076(2007).
RN [12]
RP INVOLVEMENT IN MALIGNANT MELANOMA.
RX PubMed=19097084; DOI=10.1002/jcb.21984;
RA Stevens A.P., Spangler B., Wallner S., Kreutz M., Dettmer K., Oefner P.J.,
RA Bosserhoff A.K.;
RT "Direct and tumor microenvironment mediated influences of 5'-deoxy-5'-
RT (methylthio)adenosine on tumor progression of malignant melanoma.";
RL J. Cell. Biochem. 106:210-219(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 INVOLVEMENT IN GASTRIC CANCER.
RX PubMed=21412930; DOI=10.1002/gcc.20867;
RA Kim J., Kim M.A., Min S.Y., Jee C.D., Lee H.E., Kim W.H.;
RT "Downregulation of methylthioadenosine phosphorylase by homozygous deletion
RT in gastric carcinoma.";
RL Genes Chromosomes Cancer 50:421-433(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MTA.
RX PubMed=10404592; DOI=10.1016/s0969-2126(99)80084-7;
RA Appleby T.C., Erion M.D., Ealick S.E.;
RT "The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at
RT 1.7-A resolution provides insights into substrate binding and catalysis.";
RL Structure 7:629-641(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
RX PubMed=15122881; DOI=10.1021/bi035492h;
RA Lee J.E., Settembre E.C., Cornell K.A., Riscoe M.K., Sufrin J.R.,
RA Ealick S.E., Howell P.L.;
RT "Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase
RT explains substrate preferences and identifies regions exploitable for
RT inhibitor design.";
RL Biochemistry 43:5159-5169(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=14705926; DOI=10.1021/bi0358420;
RA Singh V., Shi W., Evans G.B., Tyler P.C., Furneaux R.H., Almo S.C.,
RA Schramm V.L.;
RT "Picomolar transition state analogue inhibitors of human 5'-
RT methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-
RT A.";
RL Biochemistry 43:9-18(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 227-237.
RX PubMed=20934997; DOI=10.3324/haematol.2010.030924;
RA Bade-Doding C., Theodossis A., Gras S., Kjer-Nielsen L., Eiz-Vesper B.,
RA Seltsam A., Huyton T., Rossjohn J., McCluskey J., Blasczyk R.;
RT "The impact of human leukocyte antigen (HLA) micropolymorphism on ligand
RT specificity within the HLA-B*41 allotypic family.";
RL Haematologica 96:110-118(2011).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.
CC Involved in the breakdown of MTA, a major by-product of polyamine
CC biosynthesis. Responsible for the first step in the methionine salvage
CC pathway after MTA has been generated from S-adenosylmethionine. Has
CC broad substrate specificity with 6-aminopurine nucleosides as preferred
CC substrates. {ECO:0000255|HAMAP-Rule:MF_03155,
CC ECO:0000269|PubMed:3091600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03155};
CC -!- ACTIVITY REGULATION: Inhibited by 5'-methylthiotubercin and 5'-
CC chloroformycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for S-methyl-5'-thioadenosine {ECO:0000269|PubMed:3091600,
CC ECO:0000269|PubMed:8687427};
CC KM=580 uM for phosphate {ECO:0000269|PubMed:3091600,
CC ECO:0000269|PubMed:8687427};
CC KM=23 uM for adenine {ECO:0000269|PubMed:3091600,
CC ECO:0000269|PubMed:8687427};
CC KM=8 uM for S-methyl-5-thio-alpha-D-ribose 1-phosphate
CC {ECO:0000269|PubMed:3091600, ECO:0000269|PubMed:8687427};
CC pH dependence:
CC Optimum pH is 7.2-7.6. {ECO:0000269|PubMed:3091600,
CC ECO:0000269|PubMed:8687427};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (phosphorylase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03155}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155,
CC ECO:0000269|PubMed:10404592, ECO:0000269|PubMed:14705926,
CC ECO:0000269|PubMed:15122881, ECO:0000269|PubMed:3091600,
CC ECO:0000269|PubMed:8687427}.
CC -!- INTERACTION:
CC Q13126; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-2547776, EBI-1003700;
CC Q13126; Q9P0I2: EMC3; NbExp=3; IntAct=EBI-2547776, EBI-1054670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000255|HAMAP-
CC Rule:MF_03155}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q13126-1; Sequence=Displayed;
CC Name=2; Synonyms=MTAP_v1;
CC IsoId=Q13126-2; Sequence=VSP_044074;
CC Name=3; Synonyms=MTAP_v2;
CC IsoId=Q13126-3; Sequence=VSP_044075;
CC Name=4; Synonyms=MTAP_v3;
CC IsoId=Q13126-4; Sequence=VSP_044076;
CC Name=5; Synonyms=MTAP_v4;
CC IsoId=Q13126-5; Sequence=VSP_044071;
CC Name=6; Synonyms=MTAP_v5;
CC IsoId=Q13126-6; Sequence=VSP_044072;
CC Name=7; Synonyms=MTAP_v6;
CC IsoId=Q13126-7; Sequence=VSP_044073;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DISEASE: Diaphyseal medullary stenosis with malignant fibrous
CC histiocytoma (DMSMFH) [MIM:112250]: An autosomal dominant bone
CC dysplasia characterized by pathologic fractures due to abnormal
CC cortical growth and diaphyseal medullary stenosis. The fractures heal
CC poorly, and there is progressive bowing of the lower extremities. Some
CC patients show a limb-girdle myopathy, with muscle weakness and atrophy.
CC Approximately 35% of affected individuals develop an aggressive form of
CC bone sarcoma consistent with malignant fibrous histiocytoma or
CC osteosarcoma. {ECO:0000269|PubMed:22464254}. Note=The disease is caused
CC by variants affecting the gene represented in this entry. DMSMFH
CC causing mutations found in MTAP exon 9 result in exon skipping and
CC dysregulated alternative splicing of all MTAP isoforms
CC (PubMed:22464254). {ECO:0000269|PubMed:22464254}.
CC -!- DISEASE: Note=Loss of MTAP activity may play a role in human cancer.
CC MTAP loss has been reported in a number of cancers, including
CC osteosarcoma, malignant melanoma and gastric cancer.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}.
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DR EMBL; U22233; AAA81646.1; -; mRNA.
DR EMBL; L40432; AAG38871.1; -; mRNA.
DR EMBL; L42634; AAR24607.2; -; Genomic_DNA.
DR EMBL; L42627; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42628; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42629; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42630; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42631; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42632; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; L42633; AAR24607.2; JOINED; Genomic_DNA.
DR EMBL; HE654772; CCF77345.1; -; mRNA.
DR EMBL; HE654773; CCF77346.1; -; mRNA.
DR EMBL; HE654774; CCF77347.1; -; mRNA.
DR EMBL; HE654775; CCF77348.1; -; mRNA.
DR EMBL; HE654776; CCF77349.1; -; mRNA.
DR EMBL; HE654777; CCF77350.1; -; mRNA.
DR EMBL; AY712791; AAU04442.1; -; mRNA.
DR EMBL; AL359922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58606.1; -; Genomic_DNA.
DR EMBL; BC026106; AAH26106.1; -; mRNA.
DR CCDS; CCDS6509.1; -. [Q13126-1]
DR PIR; I38969; I38969.
DR RefSeq; NP_002442.2; NM_002451.3. [Q13126-1]
DR PDB; 1CB0; X-ray; 1.70 A; A=1-283.
DR PDB; 1CG6; X-ray; 1.70 A; A=1-283.
DR PDB; 1K27; X-ray; 1.95 A; A=1-283.
DR PDB; 1SD1; X-ray; 2.03 A; A=1-283.
DR PDB; 1SD2; X-ray; 2.10 A; A=1-283.
DR PDB; 3LN5; X-ray; 1.90 A; C=227-237.
DR PDB; 3OZC; X-ray; 1.93 A; A=1-283.
DR PDB; 3OZD; X-ray; 2.10 A; A/B=1-283.
DR PDB; 3OZE; X-ray; 2.00 A; A/B/C/D/E/F=1-283.
DR PDB; 5EUB; X-ray; 1.81 A; A=1-283.
DR PDB; 5TC5; X-ray; 1.96 A; A/B/C=1-283.
DR PDB; 5TC6; X-ray; 1.48 A; A=1-283.
DR PDB; 5TC7; X-ray; 1.75 A; A=1-283.
DR PDB; 5TC8; X-ray; 1.80 A; A=1-283.
DR PDB; 6DYZ; X-ray; 1.62 A; A=1-283.
DR PDB; 6DZ0; X-ray; 1.62 A; A=1-283.
DR PDB; 6DZ2; X-ray; 1.99 A; A/B/C=1-283.
DR PDB; 6DZ3; X-ray; 1.91 A; A/B/C=1-283.
DR PDBsum; 1CB0; -.
DR PDBsum; 1CG6; -.
DR PDBsum; 1K27; -.
DR PDBsum; 1SD1; -.
DR PDBsum; 1SD2; -.
DR PDBsum; 3LN5; -.
DR PDBsum; 3OZC; -.
DR PDBsum; 3OZD; -.
DR PDBsum; 3OZE; -.
DR PDBsum; 5EUB; -.
DR PDBsum; 5TC5; -.
DR PDBsum; 5TC6; -.
DR PDBsum; 5TC7; -.
DR PDBsum; 5TC8; -.
DR PDBsum; 6DYZ; -.
DR PDBsum; 6DZ0; -.
DR PDBsum; 6DZ2; -.
DR PDBsum; 6DZ3; -.
DR AlphaFoldDB; Q13126; -.
DR SMR; Q13126; -.
DR BioGRID; 110611; 69.
DR IntAct; Q13126; 20.
DR MINT; Q13126; -.
DR STRING; 9606.ENSP00000369519; -.
DR BindingDB; Q13126; -.
DR ChEMBL; CHEMBL4941; -.
DR DrugBank; DB02158; (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol.
DR DrugBank; DB02933; 5'-Deoxy-5'-(Methylthio)-Tubercidin.
DR DrugBank; DB02282; 5'-S-methyl-5'-thioadenosine.
DR DrugBank; DB00173; Adenine.
DR DrugBank; DB02281; Formycin.
DR GlyGen; Q13126; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13126; -.
DR MetOSite; Q13126; -.
DR PhosphoSitePlus; Q13126; -.
DR BioMuta; MTAP; -.
DR DMDM; 143811423; -.
DR REPRODUCTION-2DPAGE; Q13126; -.
DR UCD-2DPAGE; Q13126; -.
DR EPD; Q13126; -.
DR jPOST; Q13126; -.
DR MassIVE; Q13126; -.
DR MaxQB; Q13126; -.
DR PaxDb; Q13126; -.
DR PeptideAtlas; Q13126; -.
DR PRIDE; Q13126; -.
DR ProteomicsDB; 59174; -. [Q13126-1]
DR Antibodypedia; 35188; 285 antibodies from 34 providers.
DR DNASU; 4507; -.
DR Ensembl; ENST00000580900.5; ENSP00000463424.1; ENSG00000099810.21. [Q13126-3]
DR Ensembl; ENST00000644715.2; ENSP00000494373.1; ENSG00000099810.21. [Q13126-1]
DR GeneID; 4507; -.
DR KEGG; hsa:4507; -.
DR MANE-Select; ENST00000644715.2; ENSP00000494373.1; NM_002451.4; NP_002442.2.
DR UCSC; uc003zph.4; human. [Q13126-1]
DR CTD; 4507; -.
DR DisGeNET; 4507; -.
DR GeneCards; MTAP; -.
DR HGNC; HGNC:7413; MTAP.
DR HPA; ENSG00000099810; Low tissue specificity.
DR MalaCards; MTAP; -.
DR MIM; 112250; phenotype.
DR MIM; 156540; gene.
DR neXtProt; NX_Q13126; -.
DR OpenTargets; ENSG00000099810; -.
DR Orphanet; 85182; Diaphyseal medullary stenosis-bone malignancy syndrome.
DR PharmGKB; PA31220; -.
DR VEuPathDB; HostDB:ENSG00000099810; -.
DR eggNOG; KOG3985; Eukaryota.
DR GeneTree; ENSGT00950000182991; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 1616485at2759; -.
DR PhylomeDB; Q13126; -.
DR TreeFam; TF312883; -.
DR BioCyc; MetaCyc:HS01913-MON; -.
DR BRENDA; 2.4.2.28; 2681.
DR PathwayCommons; Q13126; -.
DR Reactome; R-HSA-1237112; Methionine salvage pathway.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SABIO-RK; Q13126; -.
DR SignaLink; Q13126; -.
DR UniPathway; UPA00904; UER00873.
DR BioGRID-ORCS; 4507; 39 hits in 1080 CRISPR screens.
DR ChiTaRS; MTAP; human.
DR EvolutionaryTrace; Q13126; -.
DR GeneWiki; MTAP; -.
DR GenomeRNAi; 4507; -.
DR Pharos; Q13126; Tchem.
DR PRO; PR:Q13126; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13126; protein.
DR Bgee; ENSG00000099810; Expressed in adrenal tissue and 158 other tissues.
DR ExpressionAtlas; Q13126; baseline and differential.
DR Genevisible; Q13126; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; TAS:ProtInc.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Glycosyltransferase; Nucleus; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..283
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000184545"
FT BINDING 18
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 60..61
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 93..94
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 196
FT /ligand="substrate"
FT BINDING 197
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 220..222
FT /ligand="substrate"
FT SITE 178
FT /note="Important for substrate specificity"
FT SITE 233
FT /note="Important for substrate specificity"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ65"
FT VAR_SEQ 231..283
FT /note="VSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPR
FT H -> MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGKKCLSAPAIILRPPQPR
FT GTVTTFKVSWSKDQTYICMKS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044071"
FT VAR_SEQ 231..283
FT /note="VSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPR
FT H -> MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQ
FT PMQPPCPDS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044072"
FT VAR_SEQ 232..283
FT /note="SVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
FT -> RSAFQLPP (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044073"
FT VAR_SEQ 272..283
FT /note="NMAQFSVLLPRH -> MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGR
FT GKKCLSAPAIILRPPQPRGTVTTFKVSWSKDQTYICMKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044074"
FT VAR_SEQ 272..283
FT /note="NMAQFSVLLPRH -> MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGR
FT GEILPLSPLDLAGYCFQQPMQPPCPDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044075"
FT VAR_SEQ 272..283
FT /note="NMAQFSVLLPRH -> VRSAFQLPP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:22464254"
FT /id="VSP_044076"
FT VARIANT 56
FT /note="V -> I (in dbSNP:rs7023954)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7604019, ECO:0000269|Ref.4"
FT /id="VAR_031470"
FT CONFLICT 218
FT /note="A -> G (in Ref. 2; AAG38871/AAR24607)"
FT /evidence="ECO:0000305"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6DZ3"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5TC6"
FT TURN 60..65
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6DZ3"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5TC6"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:5TC6"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6DYZ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5TC7"
FT HELIX 233..259
FT /evidence="ECO:0007829|PDB:5TC6"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:5TC6"
SQ SEQUENCE 283 AA; 31236 MW; 3B34C565EB5B99DA CRC64;
MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI KNVDCVLLAR
HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE EIQPGDIVII DQFIDRTTMR
PQSFYDGSHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMV TIEGPRFSSR
AESFMFRTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL
KENANKAKSL LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH
