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Q9CYC6

- DCP2_MOUSE

UniProt

Q9CYC6 - DCP2_MOUSE

Protein

m7GpppN-mRNA hydrolase

Gene

Dcp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety.1 Publication

    Catalytic activityi

    5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).

    Cofactori

    Manganese. Required for highest activity. Can also utilize magnesium ions By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi144 – 1441ManganeseBy similarity
    Metal bindingi148 – 1481ManganeseBy similarity

    GO - Molecular functioni

    1. m7G(5')pppN diphosphatase activity Source: UniProtKB
    2. manganese ion binding Source: InterPro
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. histone mRNA catabolic process Source: UniProtKB
    2. mRNA catabolic process Source: UniProtKB
    3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Keywords - Ligandi

    Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198696. KSRP destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    m7GpppN-mRNA hydrolase (EC:3.6.1.62)
    Alternative name(s):
    mRNA-decapping enzyme 2
    Gene namesi
    Name:Dcp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1917890. Dcp2.

    Subcellular locationi

    CytoplasmP-body By similarity. Nucleus By similarity
    Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. RISC complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422m7GpppN-mRNA hydrolasePRO_0000057052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphoserine1 Publication
    Modified residuei247 – 2471Phosphoserine1 Publication
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei276 – 2761PhosphoserineBy similarity
    Modified residuei284 – 2841PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9CYC6.
    PRIDEiQ9CYC6.

    PTM databases

    PhosphoSiteiQ9CYC6.

    Expressioni

    Tissue specificityi

    Strongly expressed in brain and testis. Weakly expressed in lung. Not detected in heart, liver, kidney and muscle (at protein level).1 Publication

    Developmental stagei

    Strongly expressed in brain, heart, liver at 14.5 and 16.5 dpc. Strongly expressed in brain at 20 dpc. Weakly expressed in heart and liver at 20 dpc (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9CYC6.
    CleanExiMM_DCP2.
    GenevestigatoriQ9CYC6.

    Interactioni

    Subunit structurei

    Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2 and UPF3B. Associates with polysomes. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus) By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with DDX17 in an RNA-dependent manner By similarity. Interacts with ZC3HAV1 By similarity. Interacts with APOBEC3G in an RNA-dependent manner By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000025350.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CYC6.
    SMRiQ9CYC6. Positions 12-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 226132Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi129 – 15022Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family. DCP2 subfamily.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0494.
    GeneTreeiENSGT00390000018878.
    HOGENOMiHOG000005974.
    HOVERGENiHBG051321.
    InParanoidiQ3TLD9.
    KOiK12613.
    OMAiIINCTIY.
    OrthoDBiEOG7XM2XP.
    TreeFamiTF314180.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR007722. mRNA_decapping_BoxA.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF05026. DCP2. 1 hit.
    PF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9CYC6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPKRLEIPG SVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY    50
    MQNTPGLPQC GIRDFAKAVF SHCPFLLPQG EDVEKILDEW KEYKMGVPTY 100
    GAIILDETLE NVLLVQGYLA KSGWGFPKGK VNKEEAPHDC AAREVFEETG 150
    FDIKDYICKD DYIELRINDQ LARLYIIPGV PKDTKFNPKT RREIRNIEWF 200
    SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS RRFGDSSDSD 250
    NGFSSAGSTP ARPTVEKLSR TKFRHSQQLF PEGSPSDQWV KHRQPLQQKS 300
    HSNHGEVSDL LKAKNQNMRG NGRKQYQDSP NQKKRANGVH GQPAKQQNPL 350
    VKCEKKLHPR KLQDNFETDA TCDLPCSGEE PSVEHAEGHS VACNGHCKFP 400
    FSSRAFLSFK FDQNAIMKIL DL 422
    Length:422
    Mass (Da):48,380
    Last modified:July 27, 2011 - v2
    Checksum:i80FE791B05E4C8FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261F → Y in BAB30946. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK017809 mRNA. Translation: BAB30946.1.
    AK166560 mRNA. Translation: BAE38853.1.
    CCDSiCCDS50275.1.
    RefSeqiNP_081766.1. NM_027490.1.
    UniGeneiMm.87629.

    Genome annotation databases

    EnsembliENSMUST00000025350; ENSMUSP00000025350; ENSMUSG00000024472.
    GeneIDi70640.
    KEGGimmu:70640.
    UCSCiuc008eux.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK017809 mRNA. Translation: BAB30946.1 .
    AK166560 mRNA. Translation: BAE38853.1 .
    CCDSi CCDS50275.1.
    RefSeqi NP_081766.1. NM_027490.1.
    UniGenei Mm.87629.

    3D structure databases

    ProteinModelPortali Q9CYC6.
    SMRi Q9CYC6. Positions 12-242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000025350.

    PTM databases

    PhosphoSitei Q9CYC6.

    Proteomic databases

    PaxDbi Q9CYC6.
    PRIDEi Q9CYC6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025350 ; ENSMUSP00000025350 ; ENSMUSG00000024472 .
    GeneIDi 70640.
    KEGGi mmu:70640.
    UCSCi uc008eux.2. mouse.

    Organism-specific databases

    CTDi 167227.
    MGIi MGI:1917890. Dcp2.

    Phylogenomic databases

    eggNOGi COG0494.
    GeneTreei ENSGT00390000018878.
    HOGENOMi HOG000005974.
    HOVERGENi HBG051321.
    InParanoidi Q3TLD9.
    KOi K12613.
    OMAi IINCTIY.
    OrthoDBi EOG7XM2XP.
    TreeFami TF314180.

    Enzyme and pathway databases

    Reactomei REACT_198696. KSRP destabilizes mRNA.

    Miscellaneous databases

    NextBioi 332021.
    PROi Q9CYC6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CYC6.
    CleanExi MM_DCP2.
    Genevestigatori Q9CYC6.

    Family and domain databases

    Gene3Di 3.90.79.10. 1 hit.
    InterProi IPR007722. mRNA_decapping_BoxA.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view ]
    Pfami PF05026. DCP2. 1 hit.
    PF00293. NUDIX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55811. SSF55811. 1 hit.
    PROSITEi PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 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.
      Tissue: Embryo.
    2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    3. "Multiple mRNA decapping enzymes in mammalian cells."
      Song M.G., Li Y., Kiledjian M.
      Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiDCP2_MOUSE
    AccessioniPrimary (citable) accession number: Q9CYC6
    Secondary accession number(s): Q3TLD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3