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Q13126

- MTAP_HUMAN

UniProt

Q13126 - MTAP_HUMAN

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MTAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    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

    Pathwayi

    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

    1. phosphorylase activity Source: ProtInc
    2. S-methyl-5-thioadenosine phosphorylase activity Source: Reactome

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. L-methionine biosynthetic process from methylthioadenosine Source: Reactome
    3. nucleobase-containing compound metabolic process Source: ProtInc
    4. polyamine metabolic process Source: Reactome
    5. purine ribonucleoside salvage Source: UniProtKB-KW
    6. small molecule metabolic process Source: Reactome
    7. sulfur amino acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01913-MONOMER.
    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7413. MTAP.

    Subcellular locationi

    Cytoplasm. Nucleus UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:112250]: An 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.1 Publication
    Note: 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).1 Publication
    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.

    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

    ArrayExpressiQ13126.
    BgeeiQ13126.
    CleanExiHS_MTAP.
    GenevestigatoriQ13126.

    Organism-specific databases

    HPAiHPA046915.

    Interactioni

    Subunit structurei

    Homotrimer.5 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi110611. 20 interactions.
    IntActiQ13126. 6 interactions.
    MINTiMINT-268764.
    STRINGi9606.ENSP00000369519.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    InParanoidiQ13126.
    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. Align

    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

    MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI    50
    KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE 100
    EIQPGDIVII DQFIDRTTMR PQSFYDGSHS CARGVCHIPM AEPFCPKTRE 150
    VLIETAKKLG LRCHSKGTMV TIEGPRFSSR AESFMFRTWG ADVINMTTVP 200
    EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL KENANKAKSL 250
    LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH 283
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi143811423.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6509.1. [Q13126-1 ]
    PIRi I38969.
    RefSeqi NP_002442.2. NM_002451.3. [Q13126-1 ]
    UniGenei Hs.193268.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CB0 X-ray 1.70 A 1-283 [» ]
    1CG6 X-ray 1.70 A 1-283 [» ]
    1K27 X-ray 1.95 A 1-283 [» ]
    1SD1 X-ray 2.03 A 1-283 [» ]
    1SD2 X-ray 2.10 A 1-283 [» ]
    3LN5 X-ray 1.90 C 227-237 [» ]
    3OZC X-ray 1.93 A 1-283 [» ]
    3OZD X-ray 2.10 A/B 1-283 [» ]
    3OZE X-ray 2.00 A/B/C/D/E/F 1-283 [» ]
    ProteinModelPortali Q13126.
    SMRi Q13126. Positions 9-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110611. 20 interactions.
    IntActi Q13126. 6 interactions.
    MINTi MINT-268764.
    STRINGi 9606.ENSP00000369519.

    Chemistry

    BindingDBi Q13126.
    ChEMBLi CHEMBL4941.
    DrugBanki DB00173. Adenine.

    PTM databases

    PhosphoSitei Q13126.

    Polymorphism databases

    DMDMi 143811423.

    2D gel databases

    REPRODUCTION-2DPAGE Q13126.
    UCD-2DPAGE Q13126.

    Proteomic databases

    MaxQBi Q13126.
    PaxDbi Q13126.
    PRIDEi Q13126.

    Protocols and materials databases

    DNASUi 4507.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380172 ; ENSP00000369519 ; ENSG00000099810 . [Q13126-1 ]
    ENST00000580900 ; ENSP00000463424 ; ENSG00000099810 . [Q13126-3 ]
    GeneIDi 4507.
    KEGGi hsa:4507.
    UCSCi uc003zph.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

    CTDi 4507.
    GeneCardsi GC09P021792.
    H-InvDB HIX0007954.
    HIX0025895.
    HGNCi HGNC:7413. MTAP.
    HPAi HPA046915.
    MIMi 112250. phenotype.
    156540. gene.
    neXtProti NX_Q13126.
    Orphaneti 85182. Diaphyseal medullary stenosis - bone malignancy.
    PharmGKBi PA31220.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0005.
    HOGENOMi HOG000228986.
    HOVERGENi HBG002487.
    InParanoidi Q13126.
    KOi K00772.
    OrthoDBi EOG771270.
    PhylomeDBi Q13126.
    TreeFami TF312883.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    BioCyci MetaCyc:HS01913-MONOMER.
    Reactomei REACT_75881. Methionine salvage pathway.
    SABIO-RK Q13126.
    SignaLinki Q13126.

    Miscellaneous databases

    ChiTaRSi MTAP. human.
    EvolutionaryTracei Q13126.
    GeneWikii MTAP.
    GenomeRNAii 4507.
    NextBioi 17416.
    PROi Q13126.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13126.
    Bgeei Q13126.
    CleanExi HS_MTAP.
    Genevestigatori Q13126.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    HAMAPi MF_01963. MTAP.
    InterProi IPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01694. MTAP. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 153 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