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Q8IU60

- DCP2_HUMAN

UniProt

Q8IU60 - DCP2_HUMAN

Protein

m7GpppN-mRNA hydrolase

Gene

DCP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      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.7 Publications

    Catalytic activityi

    5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).2 Publications

    Cofactori

    Manganese. Required for highest activity. Can also utilize magnesium ions.1 Publication

    Sites

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

    GO - Molecular functioni

    1. exoribonuclease activity, producing 5'-phosphomonoesters Source: Reactome
    2. m7G(5')pppN diphosphatase activity Source: UniProtKB
    3. manganese ion binding Source: InterPro
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. histone mRNA catabolic process Source: UniProtKB
    4. mRNA catabolic process Source: UniProtKB
    5. mRNA metabolic process Source: Reactome
    6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    8. RNA metabolic process Source: Reactome
    9. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Keywords - Ligandi

    Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18355. ATF4 activates genes.
    REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    m7GpppN-mRNA hydrolase (EC:3.6.1.62)
    Alternative name(s):
    Nucleoside diphosphate-linked moiety X motif 20
    Short name:
    Nudix motif 20
    mRNA-decapping enzyme 2
    Short name:
    hDpc
    Gene namesi
    Name:DCP2
    Synonyms:NUDT20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:24452. DCP2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: MGI
    2. cytosol Source: Reactome
    3. nucleus Source: HPA
    4. RISC complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi147 – 1471E → Q: Loss of decapping activity; when associated with Q-148. 1 Publication
    Mutagenesisi148 – 1481E → Q: Strongly reduced decapping activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134898646.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420m7GpppN-mRNA hydrolasePRO_0000057051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphoserine2 Publications
    Modified residuei247 – 2471Phosphoserine2 Publications
    Modified residuei249 – 2491Phosphoserine2 Publications
    Modified residuei276 – 2761Phosphoserine1 Publication
    Modified residuei284 – 2841Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IU60.
    PaxDbiQ8IU60.
    PRIDEiQ8IU60.

    PTM databases

    PhosphoSiteiQ8IU60.

    Expressioni

    Tissue specificityi

    Expressed in brain and testis. Not detected in heart (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ8IU60.
    BgeeiQ8IU60.
    CleanExiHS_DCP2.
    GenevestigatoriQ8IU60.

    Organism-specific databases

    HPAiCAB011677.
    HPA050694.

    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. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus). Associates with polysomes. Interacts with LIMD1, WTIP and AJUBA. Interacts with DDX17 in an RNA-dependent manner. Interacts with ZC3HAV1. Interacts with APOBEC3G in an RNA-dependent manner.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCP1AQ9NPI67EBI-521577,EBI-374238
    DCP1BQ8IZD43EBI-521577,EBI-521595
    EDC4Q6P2E94EBI-521577,EBI-1006038
    UPF1Q929003EBI-521577,EBI-373471

    Protein-protein interaction databases

    BioGridi127944. 47 interactions.
    DIPiDIP-31126N.
    IntActiQ8IU60. 11 interactions.
    STRINGi9606.ENSP00000373715.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IU60.
    SMRiQ8IU60. 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.
    HOGENOMiHOG000005974.
    HOVERGENiHBG051321.
    InParanoidiQ8IU60.
    KOiK12613.
    OMAiHSQPAKQ.
    OrthoDBiEOG7XM2XP.
    PhylomeDBiQ8IU60.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IU60-1) [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

    METKRVEIPG SVLDDFCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY    50
    MQNTPGLPQC GIRDFAKAVF SHCPFLLPQG EDVEKVLDEW KEYKMGVPTY 100
    GAIILDETLE NVLLVQGYLA KSGWGFPKGK VNKEEAPHDC AAREVFEETG 150
    FDIKDYICKD DYIELRINDQ LARLYIIPGI PKDTKFNPKT RREIRNIEWF 200
    SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS RRFGDSSDSD 250
    NGFSSTGSTP AKPTVEKLSR TKFRHSQQLF PDGSPGDQWV KHRQPLQQKP 300
    YNNHSEMSDL LKGKNQSMRG NGRKQYQDSP NQKKRTNGLQ PAKQQNSLMK 350
    CEKKLHPRKL QDNFETDAVY DLPSSSEDQL LEHAEGQPVA CNGHCKFPFS 400
    SRAFLSFKFD HNAIMKILDL 420
    Length:420
    Mass (Da):48,457
    Last modified:November 24, 2009 - v2
    Checksum:i78925E9E4FF0F6C8
    GO
    Isoform 2 (identifier: Q8IU60-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         315-349: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:385
    Mass (Da):44,443
    Checksum:i07D9868EE38D2363
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031I → V in BAC03479. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161F → L.4 Publications
    Corresponds to variant rs33555 [ dbSNP | Ensembl ].
    VAR_059528

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei315 – 34935Missing in isoform 2. 1 PublicationVSP_012908Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146650 mRNA. Translation: AAN62762.1.
    AY135173 mRNA. Translation: AAN08884.1.
    AK090564 mRNA. Translation: BAC03479.1.
    AC008536 Genomic DNA. No translation available.
    BC045596 mRNA. Translation: AAH45596.1.
    BC064593 mRNA. Translation: AAH64593.1.
    CCDSiCCDS34210.1. [Q8IU60-1]
    CCDS56377.1. [Q8IU60-2]
    RefSeqiNP_001229306.1. NM_001242377.1.
    NP_689837.2. NM_152624.5.
    UniGeneiHs.443875.

    Genome annotation databases

    EnsembliENST00000389063; ENSP00000373715; ENSG00000172795. [Q8IU60-1]
    ENST00000515408; ENSP00000425770; ENSG00000172795. [Q8IU60-2]
    GeneIDi167227.
    KEGGihsa:167227.
    UCSCiuc003kqh.3. human. [Q8IU60-1]
    uc010jcc.3. human. [Q8IU60-2]

    Polymorphism databases

    DMDMi269849560.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146650 mRNA. Translation: AAN62762.1 .
    AY135173 mRNA. Translation: AAN08884.1 .
    AK090564 mRNA. Translation: BAC03479.1 .
    AC008536 Genomic DNA. No translation available.
    BC045596 mRNA. Translation: AAH45596.1 .
    BC064593 mRNA. Translation: AAH64593.1 .
    CCDSi CCDS34210.1. [Q8IU60-1 ]
    CCDS56377.1. [Q8IU60-2 ]
    RefSeqi NP_001229306.1. NM_001242377.1.
    NP_689837.2. NM_152624.5.
    UniGenei Hs.443875.

    3D structure databases

    ProteinModelPortali Q8IU60.
    SMRi Q8IU60. Positions 12-242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127944. 47 interactions.
    DIPi DIP-31126N.
    IntActi Q8IU60. 11 interactions.
    STRINGi 9606.ENSP00000373715.

    PTM databases

    PhosphoSitei Q8IU60.

    Polymorphism databases

    DMDMi 269849560.

    Proteomic databases

    MaxQBi Q8IU60.
    PaxDbi Q8IU60.
    PRIDEi Q8IU60.

    Protocols and materials databases

    DNASUi 167227.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389063 ; ENSP00000373715 ; ENSG00000172795 . [Q8IU60-1 ]
    ENST00000515408 ; ENSP00000425770 ; ENSG00000172795 . [Q8IU60-2 ]
    GeneIDi 167227.
    KEGGi hsa:167227.
    UCSCi uc003kqh.3. human. [Q8IU60-1 ]
    uc010jcc.3. human. [Q8IU60-2 ]

    Organism-specific databases

    CTDi 167227.
    GeneCardsi GC05P112340.
    HGNCi HGNC:24452. DCP2.
    HPAi CAB011677.
    HPA050694.
    MIMi 609844. gene.
    neXtProti NX_Q8IU60.
    PharmGKBi PA134898646.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0494.
    HOGENOMi HOG000005974.
    HOVERGENi HBG051321.
    InParanoidi Q8IU60.
    KOi K12613.
    OMAi HSQPAKQ.
    OrthoDBi EOG7XM2XP.
    PhylomeDBi Q8IU60.
    TreeFami TF314180.

    Enzyme and pathway databases

    Reactomei REACT_18355. ATF4 activates genes.
    REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi DCP2. human.
    GeneWikii DCP2.
    GenomeRNAii 167227.
    NextBioi 88663.
    PROi Q8IU60.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IU60.
    Bgeei Q8IU60.
    CleanExi HS_DCP2.
    Genevestigatori Q8IU60.

    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 human decapping complex associated with hUpf proteins in nonsense-mediated decay."
      Lykke-Andersen J.
      Mol. Cell. Biol. 22:8114-8121(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF GLU-148, SUBCELLULAR LOCATION, INTERACTION WITH DCP1A AND UPF1, VARIANT LEU-16.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF 147-GLU-GLU-148, SUBCELLULAR LOCATION, ASSOCIATION WITH POLYSOMES, VARIANT LEU-16.
      Tissue: Erythroleukemia.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-16.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2), VARIANT LEU-16.
      Tissue: Blood and Uterus.
    6. "Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures."
      van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Seraphin B.
      EMBO J. 21:6915-6924(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    7. "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
      Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
      RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
    8. "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
      Lejeune F., Li X., Maquat L.E.
      Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A MRNA DECAY COMPLEX WITH UPF1; UPF2 AND UPF3B, SUBCELLULAR LOCATION.
    9. "Functional characterization of the mammalian mRNA decapping enzyme hDcp2."
      Piccirillo C., Khanna R., Kiledjian M.
      RNA 9:1138-1147(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, COFACTOR.
    10. "A protein interaction framework for human mRNA degradation."
      Lehner B., Sanderson C.M.
      Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCP1A AND DCP1B.
    11. "Cytoplasmic foci are sites of mRNA decay in human cells."
      Cougot N., Babajko S., Seraphin B.
      J. Cell Biol. 165:31-40(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCP1A.
    12. "Functional analysis of mRNA scavenger decapping enzymes."
      Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.
      RNA 10:1412-1422(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
      Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
      Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCP1A; EDC3; EDC4 AND DDX6, SUBCELLULAR LOCATION.
    14. "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
      Wichroski M.J., Robb G.B., Rana T.M.
      PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOBEC3G.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. "SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity."
      Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C.
      Biochem. Biophys. Res. Commun. 370:195-199(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM21.
    17. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247; SER-249 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    21. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZC3HAV1 AND DDX17.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCP2_HUMAN
    AccessioniPrimary (citable) accession number: Q8IU60
    Secondary accession number(s): C9J778
    , Q6P2D4, Q7Z5W5, Q8NBG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 111 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3