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Q96C86 (DCPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DCPS
Synonyms:DCS1, HINT5
ORF Names:HSPC015
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.17). 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 (Ref.8). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.17 Ref.21

Catalytic activity

A 5'-(N(7)-methyl 5'-triphosphoguanosine)-(mRNA) + H2O = N(7)-methylguanosine 5'-phosphate + a 5'-diphospho-(mRNA). Ref.9 Ref.10 Ref.17 Ref.22

Enzyme regulation

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. Ref.17 Ref.22

Subunit structure

Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1. Ref.2 Ref.7 Ref.11 Ref.20 Ref.21

Subcellular location

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. Ref.3 Ref.9 Ref.12

Tissue specificity

Detected in liver, brain, kidney, testis and prostate. Ref.3

Induction

Up-regulated by menadione. Up-regulated by the transcription factor LTF isoform delta-lactoferrin(at protein level). Ref.11 Ref.14 Ref.17 Ref.22

Domain

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. Ref.9

Sequence similarities

Belongs to the HIT family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular response to menadione

Inferred from direct assay Ref.11. Source: UniProtKB

deadenylation-dependent decapping of nuclear-transcribed mRNA

Inferred from electronic annotation. Source: InterPro

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA cis splicing, via spliceosome

Inferred from direct assay Ref.12. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of programmed cell death

Inferred from direct assay Ref.11. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement Ref.2Ref.10Ref.17. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18441014. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.3PubMed 18441014. Source: UniProtKB

   Molecular_functionRNA 7-methylguanosine cap binding

Inferred from direct assay Ref.2Ref.10Ref.12PubMed 18441014Ref.17. Source: UniProtKB

m7G(5')pppN diphosphatase activity

Inferred from direct assay Ref.2Ref.10Ref.12PubMed 18441014Ref.22Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 337336m7GpppX diphosphatase
PRO_0000109794

Regions

Region268 – 27912Substrate binding
Motif10 – 134nuclear localization signal (NLS)
Motif142 – 15413nuclear export sequence (NES)
Motif275 – 2795Histidine triad motif

Sites

Active site2771Nucleophile
Binding site1751Substrate
Binding site1851Substrate
Binding site2051Substrate
Binding site2071Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.13 Ref.18 Ref.19
Modified residue1381N6-acetyllysine Ref.15
Modified residue1421N6-acetyllysine Ref.15

Natural variations

Natural variant731G → E. Ref.5
Corresponds to variant rs11557735 [ dbSNP | Ensembl ].
VAR_027958

Experimental info

Mutagenesis10 – 134Missing: Increases cytoplasmic localization. Ref.12
Mutagenesis581R → A: Increases decapping activity to 125% of wild-type. Ref.20
Mutagenesis611I → A: No effect. Ref.20
Mutagenesis631F → A: No effect. Ref.20
Mutagenesis831I → A: Strongly reduces decapping activity. Ref.20
Mutagenesis851E → A: Reduces decapping activity. Ref.20
Mutagenesis1081F → A: Reduces decapping activity. Ref.20
Mutagenesis1101N → A: Loss of decapping activity. Ref.20
Mutagenesis1131Y → A: Loss of decapping activity. Ref.20
Mutagenesis1281K → A: No effect. Ref.20
Mutagenesis1381K → D: Increases decapping activity to 250% of wild-type. Ref.20
Mutagenesis1451R → A: Increases decapping activity to 180% of wild-type. Ref.20
Mutagenesis1461Q → P: Increases decapping activity to 140% of wild-type. Ref.20
Mutagenesis1481L → A: Inhibits nuclear export to the cytoplasm. Ref.12
Mutagenesis1501L → A: Inhibits nuclear export to the cytoplasm. Ref.12
Mutagenesis1751W → A: Loss of decapping activity. Ref.20
Mutagenesis1851E → A: Loss of decapping activity. Ref.20
Mutagenesis2041P → A: Reduces decapping activity. Ref.20
Mutagenesis2051D → A: Reduces decapping activity. Ref.20
Mutagenesis2061L → A: No effect. Ref.20
Mutagenesis2071K → A: Reduces decapping activity. Ref.20
Mutagenesis2071K → R: No effect. Ref.20
Mutagenesis2171Y → A: No effect. Ref.20
Mutagenesis2171Y → F: Reduces decapping activity. Ref.20
Mutagenesis2681H → N: Loss of decapping activity. Ref.20
Mutagenesis2721S → A: No effect. Ref.20
Mutagenesis2731Y → A: Reduces decapping activity. Ref.21
Mutagenesis2731Y → F: Activates decapping activity to 120% of wild-type. Ref.21
Mutagenesis2771H → 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). Ref.2 Ref.9 Ref.20
Mutagenesis2791H → N: Loss of decapping activity. Ref.20
Mutagenesis2941R → A or K: No effect. Ref.20
Mutagenesis3221R → A: No effect. Ref.20
Sequence conflict691N → K in AAK91763. Ref.1

Secondary structure

................................................................ 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96C86 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: C9C5A33C212D7A52

FASTA33738,609
        10         20         30         40         50         60 
MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK 

        70         80         90        100        110        120 
IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP 

       130        140        150        160        170        180 
PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL 

       190        200        210        220        230        240 
DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL 

       250        260        270        280        290        300 
LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE 

       310        320        330 
VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"DcpS as a therapeutic target for spinal muscular atrophy."
Singh J., Salcius M., Liu S.W., Staker B.L., Mishra R., Thurmond J., Michaud G., Mattoon D.R., Printen J., Christensen J., Bjornsson J.M., Pollok B.A., Kiledjian M., Stewart L., Jarecki J., Gurney M.E.
ACS Chem. Biol. 3:711-722(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-337 IN COMPLEX WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8473.1.
RefSeqNP_054745.1. NM_014026.3.
UniGeneHs.504249.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ96C86.
SMRQ96C86. Positions 38-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118787. 31 interactions.
IntActQ96C86. 4 interactions.
STRING9606.ENSP00000263579.

Chemistry

BindingDBQ96C86.
ChEMBLCHEMBL1949488.

PTM databases

PhosphoSiteQ96C86.

Polymorphism databases

DMDM116241325.

2D gel databases

REPRODUCTION-2DPAGEIPI00335385.

Proteomic databases

MaxQBQ96C86.
PaxDbQ96C86.
PeptideAtlasQ96C86.
PRIDEQ96C86.

Protocols and materials databases

DNASU28960.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263579; ENSP00000263579; ENSG00000110063.
GeneID28960.
KEGGhsa:28960.
UCSCuc001qdp.3. human.

Organism-specific databases

CTD28960.
GeneCardsGC11P126173.
HGNCHGNC:29812. DCPS.
HPAHPA039632.
MIM610534. gene.
neXtProtNX_Q96C86.
PharmGKBPA134863866.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5075.
HOGENOMHOG000182411.
HOVERGENHBG051322.
InParanoidQ96C86.
KOK12584.
OMAGENHGLW.
OrthoDBEOG7QNVMZ.
PhylomeDBQ96C86.
TreeFamTF105622.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ96C86.
CleanExHS_DCPS.
GenevestigatorQ96C86.

Family and domain databases

Gene3D3.30.428.10. 1 hit.
InterProIPR008594. DcpS/DCS2.
IPR019808. Histidine_triad_CS.
IPR011146. HIT-like.
IPR011145. Scavenger_mRNA_decap_enz_N.
[Graphical view]
PANTHERPTHR12978. PTHR12978. 1 hit.
PfamPF05652. DcpS. 1 hit.
[Graphical view]
PIRSFPIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
SUPFAMSSF102860. SSF102860. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEPS00892. HIT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCPS. human.
EvolutionaryTraceQ96C86.
GeneWikiDCPS_(gene).
GenomeRNAi28960.
NextBio51799.
PROQ96C86.
SOURCESearch...

Entry information

Entry nameDCPS_HUMAN
AccessionPrimary (citable) accession number: Q96C86
Secondary accession number(s): Q8NHL8, Q9Y2S5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM