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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MTAP

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

Functioni

Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.UniRule annotation1 Publication

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Enzyme regulationi

Inhibited by 5'-methylthiotubercin and 5'-chloroformycin.

Kineticsi

  1. KM=5 µM for S-methyl-5'-thioadenosine2 Publications
  2. KM=580 µM for phosphate2 Publications
  3. KM=23 µM for adenine2 Publications
  4. KM=8 µM for S-methyl-5-thio-alpha-D-ribose 1-phosphate2 Publications

    pH dependencei

    Optimum pH is 7.2-7.6.2 Publications

    Pathway: L-methionine biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. S-methyl-5'-thioadenosine phosphorylase (MTAP), S-methyl-5'-thioadenosine phosphorylase (MTAP), S-methyl-5'-thioadenosine phosphorylase (MTAP)
    This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181Phosphate
    Sitei178 – 1781Important for substrate specificity
    Binding sitei196 – 1961Substrate; via amide nitrogen
    Binding sitei197 – 1971Phosphate
    Sitei233 – 2331Important for substrate specificity

    GO - Molecular functioni

    • phosphorylase activity Source: ProtInc
    • S-methyl-5-thioadenosine phosphorylase activity Source: GO_Central

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01913-MONOMER.
    BRENDAi2.4.2.28. 2681.
    ReactomeiREACT_75881. Methionine salvage pathway.
    SABIO-RKQ13126.
    SignaLinkiQ13126.
    UniPathwayiUPA00904; UER00873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
    Alternative name(s):
    5'-methylthioadenosine phosphorylaseUniRule annotation
    Short name:
    MTA phosphorylaseUniRule annotation
    Short name:
    MTAPUniRule annotation
    Short name:
    MTAPaseUniRule annotation
    Gene namesi
    Name:MTAPUniRule annotation
    Synonyms:MSAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7413. MTAP.

    Subcellular locationi

    • Cytoplasm
    • Nucleus UniRule annotation

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry. DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).

    Disease descriptionAn autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma.

    See also OMIM:112250

    Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.

    Organism-specific databases

    MIMi112250. phenotype.
    Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
    PharmGKBiPA31220.

    Chemistry

    DrugBankiDB00173. Adenine.

    Polymorphism and mutation databases

    BioMutaiMTAP.
    DMDMi143811423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylasePRO_0000184545Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13126.
    PaxDbiQ13126.
    PRIDEiQ13126.

    2D gel databases

    REPRODUCTION-2DPAGEQ13126.
    UCD-2DPAGEQ13126.

    PTM databases

    PhosphoSiteiQ13126.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    BgeeiQ13126.
    CleanExiHS_MTAP.
    ExpressionAtlasiQ13126. baseline and differential.
    GenevisibleiQ13126. HS.

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPHQ9H3R53EBI-2547776,EBI-1003700

    Protein-protein interaction databases

    BioGridi110611. 22 interactions.
    IntActiQ13126. 7 interactions.
    MINTiMINT-268764.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 166Combined sources
    Helixi23 – 253Combined sources
    Beta strandi26 – 327Combined sources
    Beta strandi45 – 506Combined sources
    Beta strandi53 – 597Combined sources
    Turni60 – 656Combined sources
    Helixi69 – 713Combined sources
    Helixi74 – 8310Combined sources
    Beta strandi87 – 9711Combined sources
    Beta strandi107 – 1093Combined sources
    Beta strandi112 – 1165Combined sources
    Beta strandi126 – 1283Combined sources
    Beta strandi134 – 1363Combined sources
    Beta strandi140 – 1423Combined sources
    Helixi146 – 15813Combined sources
    Beta strandi163 – 1653Combined sources
    Beta strandi168 – 1725Combined sources
    Helixi180 – 1889Combined sources
    Beta strandi193 – 1975Combined sources
    Helixi198 – 20710Combined sources
    Beta strandi211 – 22010Combined sources
    Turni222 – 2243Combined sources
    Beta strandi225 – 2284Combined sources
    Helixi233 – 25826Combined sources
    Helixi264 – 27512Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CB0X-ray1.70A1-283[»]
    1CG6X-ray1.70A1-283[»]
    1K27X-ray1.95A1-283[»]
    1SD1X-ray2.03A1-283[»]
    1SD2X-ray2.10A1-283[»]
    3LN5X-ray1.90C227-237[»]
    3OZCX-ray1.93A1-283[»]
    3OZDX-ray2.10A/B1-283[»]
    3OZEX-ray2.00A/B/C/D/E/F1-283[»]
    ProteinModelPortaliQ13126.
    SMRiQ13126. Positions 9-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13126.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 612Phosphate binding
    Regioni93 – 942Phosphate binding
    Regioni220 – 2223Substrate binding

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0005.
    GeneTreeiENSGT00550000074874.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    KOiK00772.
    OrthoDBiEOG771270.
    PhylomeDBiQ13126.
    TreeFamiTF312883.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q13126-1) [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

            10         20         30         40         50
    MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI
    60 70 80 90 100
    KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE
    110 120 130 140 150
    EIQPGDIVII DQFIDRTTMR PQSFYDGSHS CARGVCHIPM AEPFCPKTRE
    160 170 180 190 200
    VLIETAKKLG LRCHSKGTMV TIEGPRFSSR AESFMFRTWG ADVINMTTVP
    210 220 230 240 250
    EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL KENANKAKSL
    260 270 280
    LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH
    Length:283
    Mass (Da):31,236
    Last modified:April 3, 2007 - v2
    Checksum:i3B34C565EB5B99DA
    GO
    Isoform 2 (identifier: Q13126-2) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v1

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

    Show »
    Length:346
    Mass (Da):38,356
    Checksum:i1681DA9B0DFB66EE
    GO
    Isoform 3 (identifier: Q13126-3) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v2

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQPMQPPCPDS

    Show »
    Length:334
    Mass (Da):36,936
    Checksum:i3CD3E1A173FC3465
    GO
    Isoform 4 (identifier: Q13126-4) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v3

    The sequence of this isoform differs from the canonical sequence as follows:
         272-283: NMAQFSVLLPRH → VRSAFQLPP

    Show »
    Length:280
    Mass (Da):30,838
    Checksum:i68C30E7ABA7B8AB6
    GO
    Isoform 5 (identifier: Q13126-5) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v4

    The sequence of this isoform differs from the canonical sequence as follows:
         231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...KDQTYICMKS

    Show »
    Length:305
    Mass (Da):33,797
    Checksum:iD50D41EC7E7123EB
    GO
    Isoform 6 (identifier: Q13126-6) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v5

    The sequence of this isoform differs from the canonical sequence as follows:
         231-283: VSVDRVLKTL...AQFSVLLPRH → MIKFQMILSE...QPMQPPCPDS

    Show »
    Length:293
    Mass (Da):32,376
    Checksum:i3968FB0DFD63A981
    GO
    Isoform 7 (identifier: Q13126-7) [UniParc]FASTAAdd to basket

    Also known as: MTAP_v6

    The sequence of this isoform differs from the canonical sequence as follows:
         232-283: SVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH → RSAFQLPP

    Show »
    Length:239
    Mass (Da):26,278
    Checksum:iDD08ECE4DF322F02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181A → G in AAG38871 (PubMed:8650244).Curated
    Sequence conflicti218 – 2181A → G in AAR24607 (PubMed:8650244).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561V → I.3 Publications
    Corresponds to variant rs7023954 [ dbSNP | Ensembl ].
    VAR_031470

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 5. 1 PublicationVSP_044071Add
    BLAST
    Alternative sequencei231 – 28353VSVDR…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 6. 1 PublicationVSP_044072Add
    BLAST
    Alternative sequencei232 – 28352SVDRV…LLPRH → RSAFQLPP in isoform 7. 1 PublicationVSP_044073Add
    BLAST
    Alternative sequencei272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGKKC LSAPAIILRPPQPRGTVTTF KVSWSKDQTYICMKS in isoform 2. 1 PublicationVSP_044074Add
    BLAST
    Alternative sequencei272 – 28312NMAQF…LLPRH → MIKFQMILSEGYHPFNIQES PFYRGLLDFPSVGHGRGEIL PLSPLDLAGYCFQQPMQPPC PDS in isoform 3. 1 PublicationVSP_044075Add
    BLAST
    Alternative sequencei272 – 28312NMAQF…LLPRH → VRSAFQLPP in isoform 4. 1 PublicationVSP_044076Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22233 mRNA. Translation: AAA81646.1.
    L40432 mRNA. Translation: AAG38871.1.
    L42634
    , L42627, L42628, L42629, L42630, L42631, L42632, L42633 Genomic DNA. Translation: AAR24607.2.
    HE654772 mRNA. Translation: CCF77345.1.
    HE654773 mRNA. Translation: CCF77346.1.
    HE654774 mRNA. Translation: CCF77347.1.
    HE654775 mRNA. Translation: CCF77348.1.
    HE654776 mRNA. Translation: CCF77349.1.
    HE654777 mRNA. Translation: CCF77350.1.
    AY712791 mRNA. Translation: AAU04442.1.
    AL359922 Genomic DNA. Translation: CAI16481.1.
    CH471071 Genomic DNA. Translation: EAW58606.1.
    BC026106 mRNA. Translation: AAH26106.1.
    CCDSiCCDS6509.1. [Q13126-1]
    PIRiI38969.
    RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
    UniGeneiHs.193268.

    Genome annotation databases

    EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
    ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
    GeneIDi4507.
    KEGGihsa:4507.
    UCSCiuc003zph.3. human. [Q13126-1]
    uc031tcz.1. human. [Q13126-3]
    uc031tda.1. human. [Q13126-6]
    uc031tdb.1. human. [Q13126-4]
    uc031tdc.1. human. [Q13126-2]
    uc031tdd.1. human. [Q13126-5]
    uc031tde.1. human. [Q13126-7]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22233 mRNA. Translation: AAA81646.1.
    L40432 mRNA. Translation: AAG38871.1.
    L42634
    , L42627, L42628, L42629, L42630, L42631, L42632, L42633 Genomic DNA. Translation: AAR24607.2.
    HE654772 mRNA. Translation: CCF77345.1.
    HE654773 mRNA. Translation: CCF77346.1.
    HE654774 mRNA. Translation: CCF77347.1.
    HE654775 mRNA. Translation: CCF77348.1.
    HE654776 mRNA. Translation: CCF77349.1.
    HE654777 mRNA. Translation: CCF77350.1.
    AY712791 mRNA. Translation: AAU04442.1.
    AL359922 Genomic DNA. Translation: CAI16481.1.
    CH471071 Genomic DNA. Translation: EAW58606.1.
    BC026106 mRNA. Translation: AAH26106.1.
    CCDSiCCDS6509.1. [Q13126-1]
    PIRiI38969.
    RefSeqiNP_002442.2. NM_002451.3. [Q13126-1]
    UniGeneiHs.193268.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CB0X-ray1.70A1-283[»]
    1CG6X-ray1.70A1-283[»]
    1K27X-ray1.95A1-283[»]
    1SD1X-ray2.03A1-283[»]
    1SD2X-ray2.10A1-283[»]
    3LN5X-ray1.90C227-237[»]
    3OZCX-ray1.93A1-283[»]
    3OZDX-ray2.10A/B1-283[»]
    3OZEX-ray2.00A/B/C/D/E/F1-283[»]
    ProteinModelPortaliQ13126.
    SMRiQ13126. Positions 9-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110611. 22 interactions.
    IntActiQ13126. 7 interactions.
    MINTiMINT-268764.

    Chemistry

    BindingDBiQ13126.
    ChEMBLiCHEMBL4941.
    DrugBankiDB00173. Adenine.

    PTM databases

    PhosphoSiteiQ13126.

    Polymorphism and mutation databases

    BioMutaiMTAP.
    DMDMi143811423.

    2D gel databases

    REPRODUCTION-2DPAGEQ13126.
    UCD-2DPAGEQ13126.

    Proteomic databases

    MaxQBiQ13126.
    PaxDbiQ13126.
    PRIDEiQ13126.

    Protocols and materials databases

    DNASUi4507.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380172; ENSP00000369519; ENSG00000099810. [Q13126-1]
    ENST00000580900; ENSP00000463424; ENSG00000099810. [Q13126-3]
    GeneIDi4507.
    KEGGihsa:4507.
    UCSCiuc003zph.3. human. [Q13126-1]
    uc031tcz.1. human. [Q13126-3]
    uc031tda.1. human. [Q13126-6]
    uc031tdb.1. human. [Q13126-4]
    uc031tdc.1. human. [Q13126-2]
    uc031tdd.1. human. [Q13126-5]
    uc031tde.1. human. [Q13126-7]

    Organism-specific databases

    CTDi4507.
    GeneCardsiGC09P021792.
    H-InvDBHIX0007954.
    HIX0025895.
    HGNCiHGNC:7413. MTAP.
    MIMi112250. phenotype.
    156540. gene.
    neXtProtiNX_Q13126.
    Orphaneti85182. Diaphyseal medullary stenosis - bone malignancy.
    PharmGKBiPA31220.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0005.
    GeneTreeiENSGT00550000074874.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    KOiK00772.
    OrthoDBiEOG771270.
    PhylomeDBiQ13126.
    TreeFamiTF312883.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.
    BioCyciMetaCyc:HS01913-MONOMER.
    BRENDAi2.4.2.28. 2681.
    ReactomeiREACT_75881. Methionine salvage pathway.
    SABIO-RKQ13126.
    SignaLinkiQ13126.

    Miscellaneous databases

    ChiTaRSiMTAP. human.
    EvolutionaryTraceiQ13126.
    GeneWikiiMTAP.
    GenomeRNAii4507.
    NextBioi17416.
    PROiQ13126.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ13126.
    CleanExiHS_MTAP.
    ExpressionAtlasiQ13126. baseline and differential.
    GenevisibleiQ13126. HS.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21."
      Olopade O.I., Pomykala H.M., Hagos F., Sveen L.W., Espinosa R. III, Dreyling M.H., Gursky S., Stadler W.M., le Beau M.M., Bohlander S.K.
      Proc. Natl. Acad. Sci. U.S.A. 92:6489-6493(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-56.
      Tissue: Epidermis.
    2. "Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers."
      Nobori T., Takabayashi K., Tran P., Orvis L., Batova A., Yu A.L., Carson D.A.
      Proc. Natl. Acad. Sci. U.S.A. 93:6203-6208(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Placenta.
    3. "Primate genome gain and loss: a bone dysplasia, muscular dystrophy, and bone cancer syndrome resulting from mutated retroviral-derived MTAP transcripts."
      Camacho-Vanegas O., Camacho S.C., Till J., Miranda-Lorenzo I., Terzo E., Ramirez M.C., Schramm V., Cordovano G., Watts G., Mehta S., Kimonis V., Hoch B., Philibert K.D., Raabe C.A., Bishop D.F., Glucksman M.J., Martignetti J.A.
      Am. J. Hum. Genet. 90:614-627(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7), INVOLVEMENT IN DMSMFH.
    4. "Identification of human methylthioadenosine phosphorylase (MTAP) mRNA mutation in colon cancer cell line COLO 205."
      Li Q., Cao W.-X., Zhang Y., Shi M.-M., Liu B.-Y., Zhu Z.-G., Lin Y.-Z.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-56.
      Tissue: Colon.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(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], VARIANT ILE-56.
      Tissue: Brain.
    8. "Purification and characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase from human placenta."
      Della Ragione F., Carteni-Farina M., Gragnaniello V., Schettino M.I., Zappia V.
      J. Biol. Chem. 261:12324-12329(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    9. "Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA."
      Ragione F.D., Takabayashi K., Mastropietro S., Mercurio C., Oliva A., Russo G.L., Pietra V.D., Borriello A., Nobori T., Carson D.A., Zappia V.
      Biochem. Biophys. Res. Commun. 223:514-519(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    10. "Methylthioadenosine phosphorylase gene deletions are common in osteosarcoma."
      Garcia-Castellano J.M., Villanueva A., Healey J.H., Sowers R., Cordon-Cardo C., Huvos A., Bertino J.R., Meyers P., Gorlick R.
      Clin. Cancer Res. 8:782-787(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN OSTEOSARCOMA.
    11. "Methylthioadenosine phosphorylase deficiency in Japanese osteosarcoma patients."
      Miyazaki S., Nishioka J., Shiraishi T., Matsumine A., Uchida A., Nobori T.
      Int. J. Oncol. 31:1069-1076(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN OSTEOSARCOMA.
    12. "Direct and tumor microenvironment mediated influences of 5'-deoxy-5'-(methylthio)adenosine on tumor progression of malignant melanoma."
      Stevens A.P., Spangler B., Wallner S., Kreutz M., Dettmer K., Oefner P.J., Bosserhoff A.K.
      J. Cell. Biochem. 106:210-219(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MALIGNANT MELANOMA.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Downregulation of methylthioadenosine phosphorylase by homozygous deletion in gastric carcinoma."
      Kim J., Kim M.A., Min S.Y., Jee C.D., Lee H.E., Kim W.H.
      Genes Chromosomes Cancer 50:421-433(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN GASTRIC CANCER.
    15. "The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7-A resolution provides insights into substrate binding and catalysis."
      Appleby T.C., Erion M.D., Ealick S.E.
      Structure 7:629-641(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MTA.
    16. "Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design."
      Lee J.E., Settembre E.C., Cornell K.A., Riscoe M.K., Sufrin J.R., Ealick S.E., Howell P.L.
      Biochemistry 43:5159-5169(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
    17. "Picomolar transition state analogue inhibitors of human 5'-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A."
      Singh V., Shi W., Evans G.B., Tyler P.C., Furneaux R.H., Almo S.C., Schramm V.L.
      Biochemistry 43:9-18(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
    18. "The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family."
      Bade-Doding C., Theodossis A., Gras S., Kjer-Nielsen L., Eiz-Vesper B., Seltsam A., Huyton T., Rossjohn J., McCluskey J., Blasczyk R.
      Haematologica 96:110-118(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 227-237.

    Entry informationi

    Entry nameiMTAP_HUMAN
    AccessioniPrimary (citable) accession number: Q13126
    Secondary accession number(s): I2G7M5
    , I2G7M6, I2G7M7, I2G7M8, I2G7M9, I2G7N0, Q5T3P3, Q9H010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 3, 2007
    Last modified: June 24, 2015
    This is version 162 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.