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Q9DBT5

- AMPD2_MOUSE

UniProt

Q9DBT5 - AMPD2_MOUSE

Protein

AMP deaminase 2

Gene

Ampd2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle By similarity.By similarity

    Catalytic activityi

    AMP + H2O = IMP + NH3.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi338 – 3381Zinc; catalyticBy similarity
    Metal bindingi340 – 3401Zinc; catalyticBy similarity
    Binding sitei340 – 3401SubstrateBy similarity
    Metal bindingi607 – 6071Zinc; catalyticBy similarity
    Binding sitei610 – 6101SubstrateBy similarity
    Active sitei629 – 6291Proton acceptorPROSITE-ProRule annotation
    Metal bindingi684 – 6841Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: MGI
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cyclic purine nucleotide metabolic process Source: UniProtKB
    2. energy homeostasis Source: MGI
    3. IMP biosynthetic process Source: MGI
    4. IMP salvage Source: UniProtKB-UniPathway
    5. nucleotide metabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase 2 (EC:3.5.4.6)
    Alternative name(s):
    AMP deaminase isoform L
    Gene namesi
    Name:Ampd2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:88016. Ampd2.

    Pathology & Biotechi

    Disruption phenotypei

    Mice have normal brain histology.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 798798AMP deaminase 2PRO_0000194408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei64 – 641Phosphotyrosine1 Publication
    Modified residuei70 – 701PhosphoserineBy similarity
    Modified residuei87 – 871Phosphoserine2 Publications
    Modified residuei107 – 1071PhosphothreonineBy similarity
    Modified residuei109 – 1091Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBT5.
    PaxDbiQ9DBT5.
    PRIDEiQ9DBT5.

    PTM databases

    PhosphoSiteiQ9DBT5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBT5.
    BgeeiQ9DBT5.
    CleanExiMM_AMPD2.
    GenevestigatoriQ9DBT5.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiQ9DBT5. 1 interaction.
    MINTiMINT-4616236.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBT5.
    SMRiQ9DBT5. Positions 226-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni409 – 4146Substrate bindingBy similarity
    Regioni685 – 6884Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00390000008190.
    HOGENOMiHOG000092200.
    HOVERGENiHBG050494.
    InParanoidiA2AE28.
    KOiK01490.
    OrthoDBiEOG70ZZMQ.
    TreeFamiTF300439.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 1 hit.
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBT5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF    50
    SRSLAESELR SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA 100
    KQDFLKTDSD SDLQLYKEQG EGQGDRGLWE RDVVLEREFQ RVIISGEEKC 150
    GVPFTDLLDA AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET 200
    RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG LGLRMVRGVV 250
    HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ 300
    YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL 350
    LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD 400
    RNTFHRFDKF NAKYNPIGES VLREIFIKTD NKISGKYFAH IIKEVMADLE 450
    ESKYQNAELR LSIYGRSRDE WDKLARWAVN HKVHSPNVRW LVQVPRLFDV 500
    YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH VDGFDSVDDE 550
    SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH 600
    TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI 650
    AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY 700
    SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI 750
    RRTNVPDIRV GYRYETLCQE LALITQAVQS EMLETIPEEV GIVMSPGP 798
    Length:798
    Mass (Da):92,024
    Last modified:June 1, 2001 - v1
    Checksum:i2BC4F37E4006C7D5
    GO

    Sequence cautioni

    The sequence AAH16662.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004759 mRNA. Translation: BAB23540.1.
    AK169980 mRNA. Translation: BAE41495.1.
    AL671854 Genomic DNA. Translation: CAM27248.1.
    BC016662 mRNA. Translation: AAH16662.2. Different initiation.
    BC049119 mRNA. Translation: AAH49119.1.
    CCDSiCCDS17749.1.
    RefSeqiNP_001276648.1. NM_001289719.1.
    NP_001276649.1. NM_001289720.1.
    NP_083055.1. NM_028779.5.
    UniGeneiMm.274335.
    Mm.487815.

    Genome annotation databases

    EnsembliENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
    ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
    GeneIDi109674.
    KEGGimmu:109674.
    UCSCiuc008qxz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004759 mRNA. Translation: BAB23540.1 .
    AK169980 mRNA. Translation: BAE41495.1 .
    AL671854 Genomic DNA. Translation: CAM27248.1 .
    BC016662 mRNA. Translation: AAH16662.2 . Different initiation.
    BC049119 mRNA. Translation: AAH49119.1 .
    CCDSi CCDS17749.1.
    RefSeqi NP_001276648.1. NM_001289719.1.
    NP_001276649.1. NM_001289720.1.
    NP_083055.1. NM_028779.5.
    UniGenei Mm.274335.
    Mm.487815.

    3D structure databases

    ProteinModelPortali Q9DBT5.
    SMRi Q9DBT5. Positions 226-763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DBT5. 1 interaction.
    MINTi MINT-4616236.

    PTM databases

    PhosphoSitei Q9DBT5.

    Proteomic databases

    MaxQBi Q9DBT5.
    PaxDbi Q9DBT5.
    PRIDEi Q9DBT5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102637 ; ENSMUSP00000099697 ; ENSMUSG00000027889 .
    ENSMUST00000102638 ; ENSMUSP00000099698 ; ENSMUSG00000027889 .
    GeneIDi 109674.
    KEGGi mmu:109674.
    UCSCi uc008qxz.1. mouse.

    Organism-specific databases

    CTDi 271.
    MGIi MGI:88016. Ampd2.

    Phylogenomic databases

    eggNOGi COG1816.
    GeneTreei ENSGT00390000008190.
    HOGENOMi HOG000092200.
    HOVERGENi HBG050494.
    InParanoidi A2AE28.
    KOi K01490.
    OrthoDBi EOG70ZZMQ.
    TreeFami TF300439.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .

    Miscellaneous databases

    NextBioi 362553.
    PROi Q9DBT5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBT5.
    Bgeei Q9DBT5.
    CleanExi MM_AMPD2.
    Genevestigatori Q9DBT5.

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 1 hit.
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 and NOD.
      Tissue: Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Mammary tumor.
    4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiAMPD2_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBT5
    Secondary accession number(s): A2AE28, Q91YI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 103 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