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Q9CQ65

- MTAP_MOUSE

UniProt

Q9CQ65 - MTAP_MOUSE

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

Mtap

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.UniRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181PhosphateUniRule annotation
    Sitei178 – 1781Important for substrate specificityUniRule annotation
    Binding sitei196 – 1961Substrate; via amide nitrogenUniRule annotation
    Binding sitei197 – 1971PhosphateUniRule annotation
    Sitei233 – 2331Important for substrate specificityUniRule annotation

    GO - Molecular functioni

    1. phosphorylase activity Source: InterPro
    2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
    2. purine ribonucleoside salvage Source: UniProtKB-KW
    3. response to testosterone Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    ReactomeiREACT_199099. Methionine salvage pathway.
    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:Mtap
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1914152. Mtap.

    Subcellular locationi

    Cytoplasm. Nucleus UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylasePRO_0000184546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9CQ65.
    PaxDbiQ9CQ65.
    PRIDEiQ9CQ65.

    2D gel databases

    REPRODUCTION-2DPAGEQ9CQ65.

    PTM databases

    PhosphoSiteiQ9CQ65.

    Expressioni

    Gene expression databases

    BgeeiQ9CQ65.
    CleanExiMM_MTAP.
    GenevestigatoriQ9CQ65.

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    BioGridi211799. 1 interaction.
    IntActiQ9CQ65. 2 interactions.
    MINTiMINT-1855322.
    STRINGi10090.ENSMUSP00000061092.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQ65.
    SMRiQ9CQ65. Positions 9-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0005.
    GeneTreeiENSGT00550000074874.
    HOGENOMiHOG000228986.
    HOVERGENiHBG002487.
    InParanoidiQ9CQ65.
    KOiK00772.
    OMAiCEAQLCY.
    OrthoDBiEOG771270.
    PhylomeDBiQ9CQ65.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9CQ65-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGSACTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI    50
    KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE 100
    EIQPGDMVII DQFIDRTSLR PQTFYDGSHC SARGVCHIPM AEPFCPKTRE 150
    VLIETAKKLG LRCHSKGTIV TIEGPRFSSR AESLIFRTWG ADVVNMTTVP 200
    EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDGVLKTM KENANKAKSL 250
    LLTTIPQIGS MEWSETLRNL KNMAQFSVLP PRH 283
    Length:283
    Mass (Da):31,062
    Last modified:June 1, 2001 - v1
    Checksum:iBF64441F41AE81EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056100 mRNA. Translation: BAB32865.1.
    AK005064 mRNA. Translation: BAB23788.1.
    AK011421 mRNA. Translation: BAB27609.1.
    AK167319 mRNA. Translation: BAE39421.1.
    BC003858 mRNA. Translation: AAH03858.1.
    CCDSiCCDS18349.1.
    RefSeqiNP_077753.1. NM_024433.2.
    UniGeneiMm.28500.

    Genome annotation databases

    EnsembliENSMUST00000058030; ENSMUSP00000061092; ENSMUSG00000062937.
    GeneIDi66902.
    KEGGimmu:66902.
    UCSCiuc008tof.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056100 mRNA. Translation: BAB32865.1 .
    AK005064 mRNA. Translation: BAB23788.1 .
    AK011421 mRNA. Translation: BAB27609.1 .
    AK167319 mRNA. Translation: BAE39421.1 .
    BC003858 mRNA. Translation: AAH03858.1 .
    CCDSi CCDS18349.1.
    RefSeqi NP_077753.1. NM_024433.2.
    UniGenei Mm.28500.

    3D structure databases

    ProteinModelPortali Q9CQ65.
    SMRi Q9CQ65. Positions 9-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211799. 1 interaction.
    IntActi Q9CQ65. 2 interactions.
    MINTi MINT-1855322.
    STRINGi 10090.ENSMUSP00000061092.

    Chemistry

    BindingDBi Q9CQ65.
    ChEMBLi CHEMBL2663.

    PTM databases

    PhosphoSitei Q9CQ65.

    2D gel databases

    REPRODUCTION-2DPAGE Q9CQ65.

    Proteomic databases

    MaxQBi Q9CQ65.
    PaxDbi Q9CQ65.
    PRIDEi Q9CQ65.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058030 ; ENSMUSP00000061092 ; ENSMUSG00000062937 .
    GeneIDi 66902.
    KEGGi mmu:66902.
    UCSCi uc008tof.2. mouse.

    Organism-specific databases

    CTDi 4507.
    MGIi MGI:1914152. Mtap.

    Phylogenomic databases

    eggNOGi COG0005.
    GeneTreei ENSGT00550000074874.
    HOGENOMi HOG000228986.
    HOVERGENi HBG002487.
    InParanoidi Q9CQ65.
    KOi K00772.
    OMAi CEAQLCY.
    OrthoDBi EOG771270.
    PhylomeDBi Q9CQ65.
    TreeFami TF312883.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    Reactomei REACT_199099. Methionine salvage pathway.

    Miscellaneous databases

    NextBioi 322973.
    PROi Q9CQ65.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CQ65.
    CleanExi MM_MTAP.
    Genevestigatori Q9CQ65.

    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. "Molecular characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase-deficient mutant clones of murine lymphoma cell line R1.1."
      Kadariya Y., Nishioka J., Nakamura A., Kato-Nakazawa K., Nobori T.
      Cancer Sci. 94:519-522(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo, Liver and Placenta.
    3. "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].
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiMTAP_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQ65
    Secondary accession number(s): Q3TJS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 24, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3