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P53550

- DCP2_YEAST

UniProt

P53550 - DCP2_YEAST

Protein

mRNA-decapping enzyme subunit 2

Gene

DCP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.4 Publications

    Cofactori

    Manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi149 – 1491ManganeseBy similarity
    Metal bindingi153 – 1531ManganeseBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. hydrolase activity Source: SGD
    3. m7G(5')pppN diphosphatase activity Source: SGD
    4. manganese ion binding Source: InterPro
    5. mRNA binding Source: SGD
    6. protein binding Source: IntAct

    GO - Biological processi

    1. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
    2. deadenylation-independent decapping of nuclear-transcribed mRNA Source: SGD
    3. mRNA processing Source: UniProtKB-KW
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
    5. positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
    6. stress granule assembly Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33140-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA-decapping enzyme subunit 2 (EC:3.-.-.-)
    Alternative name(s):
    Protein PSU1
    Gene namesi
    Name:DCP2
    Synonyms:PSU1
    Ordered Locus Names:YNL118C
    ORF Names:N1917
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL118c.
    SGDiS000005062. DCP2.

    Subcellular locationi

    CytoplasmP-body 1 Publication
    Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic mRNA processing body Source: SGD
    3. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. 1 Publication
    Mutagenesisi68 – 681I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. 1 Publication
    Mutagenesisi142 – 1421D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 970970mRNA-decapping enzyme subunit 2PRO_0000057054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161Phosphoserine1 Publication
    Modified residuei439 – 4391Phosphoserine1 Publication
    Modified residuei677 – 6771Phosphothreonine1 Publication
    Modified residuei679 – 6791Phosphoserine2 Publications
    Modified residuei682 – 6821Phosphoserine2 Publications
    Modified residuei751 – 7511Phosphoserine3 Publications
    Modified residuei771 – 7711Phosphoserine1 Publication
    Modified residuei773 – 7731Phosphoserine1 Publication
    Modified residuei778 – 7781Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53550.
    PeptideAtlasiP53550.

    Expressioni

    Gene expression databases

    GenevestigatoriP53550.

    Interactioni

    Subunit structurei

    Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNA, LSM2, LSM4 and LSM8. Interacts with EDC3.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCP1Q125175EBI-270,EBI-38519
    EDC3P399987EBI-270,EBI-22300

    Protein-protein interaction databases

    BioGridi35708. 153 interactions.
    DIPiDIP-969N.
    IntActiP53550. 43 interactions.
    MINTiMINT-385102.

    Structurei

    Secondary structure

    1
    970
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi105 – 1128
    Beta strandi117 – 1259
    Beta strandi132 – 1354
    Beta strandi138 – 1403
    Helixi142 – 15413
    Turni159 – 1613
    Beta strandi167 – 1726
    Beta strandi175 – 18511
    Beta strandi187 – 1893
    Beta strandi194 – 20613
    Helixi207 – 2137
    Helixi214 – 2163
    Beta strandi221 – 2233
    Helixi224 – 2274
    Helixi228 – 23710
    Helixi242 – 2443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JVBNMR-A100-245[»]
    4K6EX-ray2.10A102-245[»]
    4KG3X-ray1.70A/B/C100-245[»]
    4KG4X-ray1.80A/B100-245[»]
    ProteinModelPortaliP53550.
    SMRiP53550. Positions 14-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53550.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 228128Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi134 – 15522Nudix boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi345 – 43086Pro-richAdd
    BLAST
    Compositional biasi436 – 4394Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    GeneTreeiENSGT00390000018878.
    KOiK12613.
    OMAiPRNDASK.
    OrthoDBiEOG7P5TBG.

    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.

    P53550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW    50
    FYTDFIKLMN PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK 100
    KSIPVRGAAI FNENLSKILL VQGTESDSWS FPRGKISKDE NDIDCCIREV 150
    KEEIGFDLTD YIDDNQFIER NIQGKNYKIF LISGVSEVFN FKPQVRNEID 200
    KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ IKNEDQLKSY 250
    AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE 300
    LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM 350
    ANVFMSNPQL FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP 400
    NPMAFGVPNM HNLSGPAVSQ PFSLPPAPLP RDSGYSSSSP GQLLDILNSK 450
    KPDSNVQSSK KPKLKILQRG TDLNSIKQNN NDETAHSNSQ ALLDLLKKPT 500
    SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE TARDERNSLN 550
    VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS 600
    TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD 650
    NSKLISQDIL KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP 700
    KVKILKRGET FASLANDKKA FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ 750
    SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE NASTSSINDA NASELLGMLK 800
    QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP RTEGGPSSEM 850
    STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI 900
    LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF 950
    DVRSNGTSGS NELLSILHRK 970
    Length:970
    Mass (Da):108,667
    Last modified:October 1, 1996 - v1
    Checksum:iD53CA2C5A546FA4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti425 – 4251P → L in AAA68866. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881V → A in strain: YJM339. 1 Publication
    Natural varianti288 – 2881Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. 1 Publication
    Natural varianti301 – 3011L → H in strain: YJM280, YJM 20 and YJM339. 1 Publication
    Natural varianti319 – 3191S → P in strain: YJM627. 1 Publication
    Natural varianti494 – 4941D → N in strain: YJM339. 1 Publication
    Natural varianti505 – 5051I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. 1 Publication
    Natural varianti522 – 5221G → D in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
    Natural varianti547 – 5471N → T in strain: YJM280 and YJM320. 1 Publication
    Natural varianti567 – 5671S → R in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
    Natural varianti574 – 5741N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication
    Natural varianti577 – 5771S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. 1 Publication
    Natural varianti622 – 6221G → S in strain: V1-09 and YJM339. 1 Publication
    Natural varianti650 – 6501D → G in strain: YJM280 and YJM320. 1 Publication
    Natural varianti740 – 7401P → S in strain: YJM269 and YJM270. 1 Publication
    Natural varianti807 – 8071T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. 1 Publication
    Natural varianti823 – 8231S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication
    Natural varianti835 – 8351D → N in strain: YJM280 and YJM320. 1 Publication
    Natural varianti844 – 8441G → V in strain: V1-09. 1 Publication
    Natural varianti851 – 8511S → P in strain: YJM280, YJM320 and YJM627. 1 Publication
    Natural varianti854 – 8541M → I in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
    Natural varianti864 – 8641E → Q in strain: YJM269 and YJM270. 1 Publication
    Natural varianti865 – 8651L → S in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
    Natural varianti866 – 8661D → A in strain: YJM627.
    Natural varianti909 – 9091A → T in strain: YJM280 and YJM320. 1 Publication
    Natural varianti945 – 9451I → L in strain: YJM627. 1 Publication
    Natural varianti951 – 9511D → E in strain: V1-09. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31377 Genomic DNA. Translation: AAC99860.1.
    L43065 Genomic DNA. Translation: AAA68866.1.
    EF125216 Genomic DNA. Translation: ABN58539.1.
    EF125217 Genomic DNA. Translation: ABN58548.1.
    EF125218 Genomic DNA. Translation: ABN58557.1.
    EF125219 Genomic DNA. Translation: ABN58566.1.
    EF125220 Genomic DNA. Translation: ABN58578.1.
    EF125221 Genomic DNA. Translation: ABN58584.1.
    EF125222 Genomic DNA. Translation: ABN58593.1.
    EF125223 Genomic DNA. Translation: ABN58602.1.
    EF125224 Genomic DNA. Translation: ABN58611.1.
    EF125225 Genomic DNA. Translation: ABN58620.1.
    EF125226 Genomic DNA. Translation: ABN58629.1.
    EF125228 Genomic DNA. Translation: ABN58647.1.
    Z69382 Genomic DNA. Translation: CAA93389.1.
    Z71394 Genomic DNA. Translation: CAA95998.1.
    BK006947 Genomic DNA. Translation: DAA10430.1.
    PIRiS63059.
    RefSeqiNP_014281.1. NM_001182956.1.

    Genome annotation databases

    EnsemblFungiiYNL118C; YNL118C; YNL118C.
    GeneIDi855605.
    KEGGisce:YNL118C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31377 Genomic DNA. Translation: AAC99860.1 .
    L43065 Genomic DNA. Translation: AAA68866.1 .
    EF125216 Genomic DNA. Translation: ABN58539.1 .
    EF125217 Genomic DNA. Translation: ABN58548.1 .
    EF125218 Genomic DNA. Translation: ABN58557.1 .
    EF125219 Genomic DNA. Translation: ABN58566.1 .
    EF125220 Genomic DNA. Translation: ABN58578.1 .
    EF125221 Genomic DNA. Translation: ABN58584.1 .
    EF125222 Genomic DNA. Translation: ABN58593.1 .
    EF125223 Genomic DNA. Translation: ABN58602.1 .
    EF125224 Genomic DNA. Translation: ABN58611.1 .
    EF125225 Genomic DNA. Translation: ABN58620.1 .
    EF125226 Genomic DNA. Translation: ABN58629.1 .
    EF125228 Genomic DNA. Translation: ABN58647.1 .
    Z69382 Genomic DNA. Translation: CAA93389.1 .
    Z71394 Genomic DNA. Translation: CAA95998.1 .
    BK006947 Genomic DNA. Translation: DAA10430.1 .
    PIRi S63059.
    RefSeqi NP_014281.1. NM_001182956.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JVB NMR - A 100-245 [» ]
    4K6E X-ray 2.10 A 102-245 [» ]
    4KG3 X-ray 1.70 A/B/C 100-245 [» ]
    4KG4 X-ray 1.80 A/B 100-245 [» ]
    ProteinModelPortali P53550.
    SMRi P53550. Positions 14-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35708. 153 interactions.
    DIPi DIP-969N.
    IntActi P53550. 43 interactions.
    MINTi MINT-385102.

    Proteomic databases

    MaxQBi P53550.
    PeptideAtlasi P53550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL118C ; YNL118C ; YNL118C .
    GeneIDi 855605.
    KEGGi sce:YNL118C.

    Organism-specific databases

    CYGDi YNL118c.
    SGDi S000005062. DCP2.

    Phylogenomic databases

    GeneTreei ENSGT00390000018878.
    KOi K12613.
    OMAi PRNDASK.
    OrthoDBi EOG7P5TBG.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33140-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P53550.
    NextBioi 979774.

    Gene expression databases

    Genevestigatori P53550.

    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. "Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen."
      He F., Jacobson A.
      Genes Dev. 9:437-454(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Tzagoloff A.A.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 24657 / D273-10B.
    3. "Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast."
      Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M.
      Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-188; ASN-288 DEL; HIS-301; PRO-319; ASN-494; THR-505; ASP-522; THR-547; ARG-567; SER-574; ASN-577; SER-622; GLY-650; SER-740; ALA-807; PRO-823; ASN-835; VAL-844; PRO-851; ILE-854; GLN-864; SER-865; THR-909; LEU-945 AND GLU-951.
      Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
    4. "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames."
      de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G.
      Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "Crystal structure of human Edc3 and its functional implications."
      Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.
      Mol. Cell. Biol. 28:5965-5976(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EDC3.
    8. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    9. "The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif."
      Dunckley T., Parker R.
      EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DCP1.
    10. "Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins."
      Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P.
      Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LSM2; LSM4 AND LSM8.
    11. "Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae."
      Dunckley T., Tucker M., Parker R.
      Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASN-60; ILE-68 AND ASP-142, INTERACTION WITH EDC1.
    12. "Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
      Tharun S., Parker R.
      Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
    15. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
      Sheth U., Parker R.
      Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "Crystal structure of Dcp1p and its functional implications in mRNA decapping."
      She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H.
      Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCP1.
    17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-682 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; THR-677; SER-679; SER-682; SER-751; SER-771; SER-773 AND SER-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: STRUCTURE BY NMR OF 100-245.

    Entry informationi

    Entry nameiDCP2_YEAST
    AccessioniPrimary (citable) accession number: P53550
    Secondary accession number(s): B0KZS6
    , B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8530 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3