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Q96C86

- DCPS_HUMAN

UniProt

Q96C86 - DCPS_HUMAN

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Protein

m7GpppX diphosphatase

Gene
DCPS, DCS1, HINT5, HSPC015
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 (1 Publication). 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 (1 Publication). 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 – 1751Substrate
Binding sitei185 – 1851Substrate
Binding sitei205 – 2051Substrate
Binding sitei207 – 2071Substrate
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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 134Missing: Increases cytoplasmic localization. 1 Publication
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 – 11Removed1 Publication
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).4 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 NDOR1.5 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.

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.

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

Natural variant

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 122 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

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