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Q96C86

- DCPS_HUMAN

UniProt

Q96C86 - DCPS_HUMAN

Protein

m7GpppX diphosphatase

Gene

DCPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death.10 Publications

    Catalytic activityi

    A 5'-(N(7)-methyl 5'-triphosphoguanosine)-(mRNA) + H2O = N(7)-methylguanosine 5'-phosphate + a 5'-diphospho-(mRNA).4 Publications

    Enzyme regulationi

    The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro. Inhibited by 2,4-diaminoquinazoline.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei175 – 1751Substrate2 Publications
    Binding sitei185 – 1851Substrate2 Publications
    Binding sitei205 – 2051Substrate2 Publications
    Binding sitei207 – 2071Substrate2 Publications
    Active sitei277 – 2771Nucleophile

    GO - Molecular functioni

    1. m7G(5')pppN diphosphatase activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA 7-methylguanosine cap binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to menadione Source: UniProtKB
    2. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: InterPro
    3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    4. gene expression Source: Reactome
    5. mRNA cis splicing, via spliceosome Source: UniProtKB
    6. mRNA metabolic process Source: Reactome
    7. negative regulation of programmed cell death Source: UniProtKB
    8. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
    9. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    ReactomeiREACT_20619. mRNA decay by 3' to 5' exoribonuclease.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    m7GpppX diphosphatase (EC:3.6.1.59)
    Alternative name(s):
    DCS-1
    Decapping scavenger enzyme
    Hint-related 7meGMP-directed hydrolase
    Histidine triad nucleotide-binding protein 5
    Histidine triad protein member 5
    Short name:
    HINT-5
    Scavenger mRNA-decapping enzyme DcpS
    Gene namesi
    Name:DCPS
    Synonyms:DCS1, HINT5
    ORF Names:HSPC015
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29812. DCPS.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. mitochondrion Source: HPA
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 134Missing: Increases cytoplasmic localization.
    Mutagenesisi58 – 581R → A: Increases decapping activity to 125% of wild-type. 1 Publication
    Mutagenesisi61 – 611I → A: No effect. 1 Publication
    Mutagenesisi63 – 631F → A: No effect. 1 Publication
    Mutagenesisi83 – 831I → A: Strongly reduces decapping activity. 1 Publication
    Mutagenesisi85 – 851E → A: Reduces decapping activity. 1 Publication
    Mutagenesisi108 – 1081F → A: Reduces decapping activity. 1 Publication
    Mutagenesisi110 – 1101N → A: Loss of decapping activity. 1 Publication
    Mutagenesisi113 – 1131Y → A: Loss of decapping activity. 1 Publication
    Mutagenesisi128 – 1281K → A: No effect. 1 Publication
    Mutagenesisi138 – 1381K → D: Increases decapping activity to 250% of wild-type. 1 Publication
    Mutagenesisi145 – 1451R → A: Increases decapping activity to 180% of wild-type. 1 Publication
    Mutagenesisi146 – 1461Q → P: Increases decapping activity to 140% of wild-type. 1 Publication
    Mutagenesisi148 – 1481L → A: Inhibits nuclear export to the cytoplasm. 1 Publication
    Mutagenesisi150 – 1501L → A: Inhibits nuclear export to the cytoplasm. 1 Publication
    Mutagenesisi175 – 1751W → A: Loss of decapping activity. 1 Publication
    Mutagenesisi185 – 1851E → A: Loss of decapping activity. 1 Publication
    Mutagenesisi204 – 2041P → A: Reduces decapping activity. 1 Publication
    Mutagenesisi205 – 2051D → A: Reduces decapping activity. 1 Publication
    Mutagenesisi206 – 2061L → A: No effect. 1 Publication
    Mutagenesisi207 – 2071K → A: Reduces decapping activity. 1 Publication
    Mutagenesisi207 – 2071K → R: No effect. 1 Publication
    Mutagenesisi217 – 2171Y → A: No effect. 1 Publication
    Mutagenesisi217 – 2171Y → F: Reduces decapping activity. 1 Publication
    Mutagenesisi268 – 2681H → N: Loss of decapping activity. 1 Publication
    Mutagenesisi272 – 2721S → A: No effect. 1 Publication
    Mutagenesisi273 – 2731Y → A: Reduces decapping activity. 1 Publication
    Mutagenesisi273 – 2731Y → F: Activates decapping activity to 120% of wild-type. 1 Publication
    Mutagenesisi277 – 2771H → N: Loss of decapping activity. Does not inhibit cap structure and capped RNA binding. Preferentially hydrolyzes cap structure (m7GpppG) at least 2500-fold more efficiently than capped RNA (m7Gppp-RNA). 3 Publications
    Mutagenesisi279 – 2791H → N: Loss of decapping activity. 1 Publication
    Mutagenesisi294 – 2941R → A or K: No effect. 1 Publication
    Mutagenesisi322 – 3221R → A: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA134863866.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 337336m7GpppX diphosphatasePRO_0000109794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei138 – 1381N6-acetyllysine1 Publication
    Modified residuei142 – 1421N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96C86.
    PaxDbiQ96C86.
    PeptideAtlasiQ96C86.
    PRIDEiQ96C86.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00335385.

    PTM databases

    PhosphoSiteiQ96C86.

    Expressioni

    Tissue specificityi

    Detected in liver, brain, kidney, testis and prostate.1 Publication

    Inductioni

    Up-regulated by menadione. Up-regulated by the transcription factor LTF isoform delta-lactoferrin (at protein level).2 Publications

    Gene expression databases

    BgeeiQ96C86.
    CleanExiHS_DCPS.
    GenevestigatoriQ96C86.

    Organism-specific databases

    HPAiHPA039632.

    Interactioni

    Subunit structurei

    Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1.6 Publications

    Protein-protein interaction databases

    BioGridi118787. 32 interactions.
    IntActiQ96C86. 4 interactions.
    STRINGi9606.ENSP00000263579.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 453
    Beta strandi48 – 569
    Turni57 – 604
    Beta strandi61 – 677
    Beta strandi79 – 868
    Helixi91 – 988
    Beta strandi103 – 1108
    Beta strandi113 – 1197
    Helixi122 – 1243
    Beta strandi127 – 1326
    Helixi137 – 1437
    Beta strandi148 – 1536
    Helixi155 – 1606
    Helixi162 – 1676
    Helixi174 – 1807
    Beta strandi183 – 1853
    Helixi186 – 1883
    Beta strandi191 – 1933
    Turni196 – 1983
    Beta strandi200 – 2045
    Helixi213 – 2153
    Beta strandi217 – 2259
    Helixi230 – 2323
    Helixi235 – 2373
    Helixi238 – 25619
    Helixi260 – 2623
    Beta strandi263 – 2708
    Beta strandi272 – 2754
    Beta strandi277 – 2826
    Turni292 – 2943
    Beta strandi295 – 2973
    Helixi298 – 30710
    Helixi311 – 3144
    Beta strandi317 – 3226
    Helixi326 – 3338

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ST0X-ray1.90A/B1-337[»]
    1ST4X-ray2.02A/B1-337[»]
    1XMLX-ray2.00A/B1-337[»]
    1XMMX-ray2.50A/B/C/D1-337[»]
    3BL7X-ray2.31A/B38-337[»]
    3BL9X-ray1.80A/B38-337[»]
    3BLAX-ray2.60A/B38-337[»]
    ProteinModelPortaliQ96C86.
    SMRiQ96C86. Positions 38-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96C86.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni268 – 27912Substrate bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi10 – 134nuclear localization signal (NLS)
    Motifi142 – 15413nuclear export sequence (NES)Add
    BLAST
    Motifi275 – 2795Histidine triad motif

    Domaini

    The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures.1 Publication

    Sequence similaritiesi

    Belongs to the HIT family.Curated

    Phylogenomic databases

    eggNOGiCOG5075.
    HOGENOMiHOG000182411.
    HOVERGENiHBG051322.
    InParanoidiQ96C86.
    KOiK12584.
    OMAiGENHGLW.
    OrthoDBiEOG7QNVMZ.
    PhylomeDBiQ96C86.
    TreeFamiTF105622.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR008594. DcpS/DCS2.
    IPR019808. Histidine_triad_CS.
    IPR011146. HIT-like.
    IPR011145. Scavenger_mRNA_decap_enz_N.
    [Graphical view]
    PANTHERiPTHR12978. PTHR12978. 1 hit.
    PfamiPF05652. DcpS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
    SUPFAMiSSF102860. SSF102860. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEiPS00892. HIT_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96C86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ    50
    KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG 100
    SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL 150
    IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF 200
    VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE 250
    AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE 300
    VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS 337
    Length:337
    Mass (Da):38,609
    Last modified:October 17, 2006 - v2
    Checksum:iC9C5A33C212D7A52
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691N → K in AAK91763. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731G → E.1 Publication
    Corresponds to variant rs11557735 [ dbSNP | Ensembl ].
    VAR_027958

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AH010984 Genomic DNA. Translation: AAK91763.1.
    AY040771 mRNA. Translation: AAK91765.1.
    AF532613 mRNA. Translation: AAM90310.1.
    AY077684 mRNA. Translation: AAL77216.1.
    AF077201 mRNA. Translation: AAD26996.1.
    BC014532 mRNA. Translation: AAH14532.1.
    CCDSiCCDS8473.1.
    RefSeqiNP_054745.1. NM_014026.3.
    UniGeneiHs.504249.

    Genome annotation databases

    EnsembliENST00000263579; ENSP00000263579; ENSG00000110063.
    GeneIDi28960.
    KEGGihsa:28960.
    UCSCiuc001qdp.3. human.

    Polymorphism databases

    DMDMi116241325.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AH010984 Genomic DNA. Translation: AAK91763.1 .
    AY040771 mRNA. Translation: AAK91765.1 .
    AF532613 mRNA. Translation: AAM90310.1 .
    AY077684 mRNA. Translation: AAL77216.1 .
    AF077201 mRNA. Translation: AAD26996.1 .
    BC014532 mRNA. Translation: AAH14532.1 .
    CCDSi CCDS8473.1.
    RefSeqi NP_054745.1. NM_014026.3.
    UniGenei Hs.504249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ST0 X-ray 1.90 A/B 1-337 [» ]
    1ST4 X-ray 2.02 A/B 1-337 [» ]
    1XML X-ray 2.00 A/B 1-337 [» ]
    1XMM X-ray 2.50 A/B/C/D 1-337 [» ]
    3BL7 X-ray 2.31 A/B 38-337 [» ]
    3BL9 X-ray 1.80 A/B 38-337 [» ]
    3BLA X-ray 2.60 A/B 38-337 [» ]
    ProteinModelPortali Q96C86.
    SMRi Q96C86. Positions 38-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118787. 32 interactions.
    IntActi Q96C86. 4 interactions.
    STRINGi 9606.ENSP00000263579.

    Chemistry

    BindingDBi Q96C86.
    ChEMBLi CHEMBL1949488.

    PTM databases

    PhosphoSitei Q96C86.

    Polymorphism databases

    DMDMi 116241325.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00335385.

    Proteomic databases

    MaxQBi Q96C86.
    PaxDbi Q96C86.
    PeptideAtlasi Q96C86.
    PRIDEi Q96C86.

    Protocols and materials databases

    DNASUi 28960.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263579 ; ENSP00000263579 ; ENSG00000110063 .
    GeneIDi 28960.
    KEGGi hsa:28960.
    UCSCi uc001qdp.3. human.

    Organism-specific databases

    CTDi 28960.
    GeneCardsi GC11P126173.
    HGNCi HGNC:29812. DCPS.
    HPAi HPA039632.
    MIMi 610534. gene.
    neXtProti NX_Q96C86.
    PharmGKBi PA134863866.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5075.
    HOGENOMi HOG000182411.
    HOVERGENi HBG051322.
    InParanoidi Q96C86.
    KOi K12584.
    OMAi GENHGLW.
    OrthoDBi EOG7QNVMZ.
    PhylomeDBi Q96C86.
    TreeFami TF105622.

    Enzyme and pathway databases

    Reactomei REACT_20619. mRNA decay by 3' to 5' exoribonuclease.

    Miscellaneous databases

    ChiTaRSi DCPS. human.
    EvolutionaryTracei Q96C86.
    GeneWikii DCPS_(gene).
    GenomeRNAii 28960.
    NextBioi 51799.
    PROi Q96C86.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96C86.
    CleanExi HS_DCPS.
    Genevestigatori Q96C86.

    Family and domain databases

    Gene3Di 3.30.428.10. 1 hit.
    InterProi IPR008594. DcpS/DCS2.
    IPR019808. Histidine_triad_CS.
    IPR011146. HIT-like.
    IPR011145. Scavenger_mRNA_decap_enz_N.
    [Graphical view ]
    PANTHERi PTHR12978. PTHR12978. 1 hit.
    Pfami PF05652. DcpS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
    SUPFAMi SSF102860. SSF102860. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEi PS00892. HIT_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel member of the histidine triad protein family (HINT-5) in different vertebrate species."
      Huang C.-H., Peng J., Chen H., Chen Y.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases."
      Liu H., Rodgers N.D., Jiao X., Kiledjian M.
      EMBO J. 21:4699-4708(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF HIS-277, SUBUNIT.
    3. "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1."
      Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R.
      J. Biol. Chem. 278:39051-39058(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    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], VARIANT GLU-73.
      Tissue: Bone marrow.
    6. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 129-138 AND 243-255, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Functional link between the mammalian exosome and mRNA decapping."
      Wang Z., Kiledjian M.
      Cell 107:751-762(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EXOSOME PROTEINS.
    8. "DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway."
      van Dijk E., Le Hir H., Seraphin B.
      Proc. Natl. Acad. Sci. U.S.A. 100:12081-12086(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-277.
    10. "Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris embryos and characterization of C. elegans scavenger DcpS."
      Cohen L.S., Mikhli C., Friedman C., Jankowska-Anyszka M., Stepinski J., Darzynkiewicz E., Davis R.E.
      RNA 10:1609-1624(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    11. "Role of a novel dual flavin reductase (NR1) and an associated histidine triad protein (DCS-1) in menadione-induced cytotoxicity."
      Kwasnicka-Crawford D.A., Vincent S.R.
      Biochem. Biophys. Res. Commun. 336:565-571(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOTOXICITY INHIBITION, INDUCTION, INTERACTION WITH NDOR1.
    12. "DcpS scavenger decapping enzyme can modulate pre-mRNA splicing."
      Shen V., Liu H., Liu S.W., Jiao X., Kiledjian M.
      RNA 14:1132-1142(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SPLICING, MUTAGENESIS OF 10-LYS--ARG-13; LEU-148 AND LEU-150, SUBCELLULAR LOCATION.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Proteomic approach to the identification of novel delta-lactoferrin target genes: Characterization of DcpS, an mRNA scavenger decapping enzyme."
      Mariller C., Hardiville S., Hoedt E., Benaissa M., Mazurier J., Pierce A.
      Biochimie 91:109-122(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly bound by decapping scavenger (dcpS) enzymes and potently inhibits their activity."
      Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J., Jemielity J., Davis R.E., Darzynkiewicz E.
      Biochemistry 51:8003-8013(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity."
      Gu M., Fabrega C., Liu S.-W., Liu H., Kiledjian M., Lima C.D.
      Mol. Cell 14:67-80(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-277 IN COMPLEX WITH SUBSTRATE, SUBUNIT, MUTAGENESIS OF ARG-58; ILE-61; PHE-63; ILE-83; GLU-85; PHE-108; ASN-110; TYR-113; LYS-128; LYS-138; ARG-145; GLN-146; TRP-175; GLU-185; PRO-204; ASP-205; LEU-206; LYS-207; TYR-217; HIS-268; SER-272; HIS-277; HIS-279; ARG-294 AND ARG-322.
    21. "Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping."
      Chen N., Walsh M.A., Liu Y., Parker R., Song H.
      J. Mol. Biol. 347:707-718(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, SUBUNIT, MUTAGENESIS OF TYR-273.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-337 IN COMPLEX WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ENZYME REGULATION.

    Entry informationi

    Entry nameiDCPS_HUMAN
    AccessioniPrimary (citable) accession number: Q96C86
    Secondary accession number(s): Q8NHL8, Q9Y2S5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 123 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3