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Entry version 158 (08 May 2019)
Sequence version 2 (17 Oct 2006)
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Protein

m7GpppX diphosphatase

Gene

DCPS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei175Substrate2 Publications1
Binding sitei185Substrate2 Publications1
Binding sitei205Substrate2 Publications1
Binding sitei207Substrate2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei277Nucleophile1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.1.59 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-429958 mRNA decay by 3' to 5' exoribonuclease

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DCPS
Synonyms:DCS1, HINT5
ORF Names:HSPC015
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:29812 DCPS

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610534 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q96C86

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Al-Raqad syndrome (ARS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by delayed psychomotor development, moderate to severe intellectual disability, poor or absent speech, microcephaly, congenital hypotonia, and severe growth delay.
See also OMIM:616459
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073956316T → M in ARS; results in a severe decrease of decapase activity. 1 PublicationCorresponds to variant dbSNP:rs137941190EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi10 – 13Missing : Increases cytoplasmic localization. 1 Publication4
Mutagenesisi58R → A: Increases decapping activity to 125% of wild-type. 1 Publication1
Mutagenesisi61I → A: No effect. 1 Publication1
Mutagenesisi63F → A: No effect. 1 Publication1
Mutagenesisi83I → A: Strongly reduces decapping activity. 1 Publication1
Mutagenesisi85E → A: Reduces decapping activity. 1 Publication1
Mutagenesisi108F → A: Reduces decapping activity. 1 Publication1
Mutagenesisi110N → A: Loss of decapping activity. 1 Publication1
Mutagenesisi113Y → A: Loss of decapping activity. 1 Publication1
Mutagenesisi128K → A: No effect. 1 Publication1
Mutagenesisi138K → D: Increases decapping activity to 250% of wild-type. 1 Publication1
Mutagenesisi145R → A: Increases decapping activity to 180% of wild-type. 1 Publication1
Mutagenesisi146Q → P: Increases decapping activity to 140% of wild-type. 1 Publication1
Mutagenesisi148L → A: Inhibits nuclear export to the cytoplasm. 1 Publication1
Mutagenesisi150L → A: Inhibits nuclear export to the cytoplasm. 1 Publication1
Mutagenesisi175W → A: Loss of decapping activity. 1 Publication1
Mutagenesisi185E → A: Loss of decapping activity. 1 Publication1
Mutagenesisi204P → A: Reduces decapping activity. 1 Publication1
Mutagenesisi205D → A: Reduces decapping activity. 1 Publication1
Mutagenesisi206L → A: No effect. 1 Publication1
Mutagenesisi207K → A: Reduces decapping activity. 1 Publication1
Mutagenesisi207K → R: No effect. 1 Publication1
Mutagenesisi217Y → A: No effect. 1 Publication1
Mutagenesisi217Y → F: Reduces decapping activity. 1 Publication1
Mutagenesisi268H → N: Loss of decapping activity. 1 Publication1
Mutagenesisi272S → A: No effect. 1 Publication1
Mutagenesisi273Y → A: Reduces decapping activity. 1 Publication1
Mutagenesisi273Y → F: Activates decapping activity to 120% of wild-type. 1 Publication1
Mutagenesisi277H → 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 Publications1
Mutagenesisi279H → N: Loss of decapping activity. 1 Publication1
Mutagenesisi294R → A or K: No effect. 1 Publication1
Mutagenesisi322R → A: No effect. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
28960

MalaCards human disease database

More...
MalaCardsi
DCPS
MIMi616459 phenotype

Open Targets

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OpenTargetsi
ENSG00000110063

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
88616 Autosomal recessive non-syndromic intellectual disability

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134863866

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1949488

Drug and drug target database

More...
DrugBanki
DB01649 7-Methyl-Gpppa
DB03958 7-methyl-guanosine-5'-triphosphate-5'-guanosine
DB01960 7n-Methyl-8-Hydroguanosine-5'-Diphosphate
DB03593 N7-Methyl-Guanosine-5'-Monophosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DCPS

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116241325

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001097942 – 337m7GpppX diphosphataseAdd BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei24PhosphoserineCombined sources1
Modified residuei101PhosphoserineBy similarity1
Modified residuei138N6-acetyllysineCombined sources1
Modified residuei142N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q96C86

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q96C86

MaxQB - The MaxQuant DataBase

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MaxQBi
Q96C86

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q96C86

PeptideAtlas

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PeptideAtlasi
Q96C86

PRoteomics IDEntifications database

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PRIDEi
Q96C86

ProteomicsDB human proteome resource

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ProteomicsDBi
76164

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00335385

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q96C86

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q96C86

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000110063 Expressed in 191 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96C86 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA039632
HPA058597

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
118787, 38 interactors

Protein interaction database and analysis system

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IntActi
Q96C86, 7 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000263579

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q96C86

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
4QDEX-ray2.90A/B/C/D2-337[»]
4QDVX-ray2.80A/B/C/D2-337[»]
4QEBX-ray3.21A/B/C/D2-337[»]
5OSYX-ray2.06A/B37-337[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q96C86

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q96C86

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni268 – 279Substrate bindingAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi10 – 13nuclear localization signal (NLS)4
Motifi142 – 154nuclear export sequence (NES)Add BLAST13
Motifi275 – 279Histidine triad motif5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HIT family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3969 Eukaryota
COG5075 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000003924

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000182411

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96C86

KEGG Orthology (KO)

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KOi
K12584

Identification of Orthologs from Complete Genome Data

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OMAi
IWCEKSH

Database of Orthologous Groups

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OrthoDBi
930557at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q96C86

TreeFam database of animal gene trees

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TreeFami
TF105622

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.200.40, 1 hit
3.30.428.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008594 DcpS/DCS2
IPR019808 Histidine_triad_CS
IPR036265 HIT-like_sf
IPR011145 Scavenger_mRNA_decap_enz_N

The PANTHER Classification System

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PANTHERi
PTHR12978 PTHR12978, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF05652 DcpS, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF028973 Scavenger_mRNA_decap_enz, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF102860 SSF102860, 1 hit
SSF54197 SSF54197, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00892 HIT_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q96C86-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ
60 70 80 90 100
KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG
110 120 130 140 150
SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL
160 170 180 190 200
IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF
210 220 230 240 250
VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE
260 270 280 290 300
AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE
310 320 330
VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS
Length:337
Mass (Da):38,609
Last modified:October 17, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC9C5A33C212D7A52
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3B3ITF0A0A3B3ITF0_HUMAN
m7GpppX diphosphatase
DCPS
244Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti69N → K in AAK91763 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02795873G → E1 PublicationCorresponds to variant dbSNP:rs11557735Ensembl.1
Natural variantiVAR_073956316T → M in ARS; results in a severe decrease of decapase activity. 1 PublicationCorresponds to variant dbSNP:rs137941190EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS8473.1

NCBI Reference Sequences

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RefSeqi
NP_054745.1, NM_014026.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000263579; ENSP00000263579; ENSG00000110063

Database of genes from NCBI RefSeq genomes

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GeneIDi
28960

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:28960

UCSC genome browser

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UCSCi
uc001qdp.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_014026.4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QDEX-ray2.90A/B/C/D2-337[»]
4QDVX-ray2.80A/B/C/D2-337[»]
4QEBX-ray3.21A/B/C/D2-337[»]
5OSYX-ray2.06A/B37-337[»]
SMRiQ96C86
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118787, 38 interactors
IntActiQ96C86, 7 interactors
STRINGi9606.ENSP00000263579

Chemistry databases

BindingDBiQ96C86
ChEMBLiCHEMBL1949488
DrugBankiDB01649 7-Methyl-Gpppa
DB03958 7-methyl-guanosine-5'-triphosphate-5'-guanosine
DB01960 7n-Methyl-8-Hydroguanosine-5'-Diphosphate
DB03593 N7-Methyl-Guanosine-5'-Monophosphate

PTM databases

iPTMnetiQ96C86
PhosphoSitePlusiQ96C86

Polymorphism and mutation databases

BioMutaiDCPS
DMDMi116241325

2D gel databases

REPRODUCTION-2DPAGEiIPI00335385

Proteomic databases

EPDiQ96C86
jPOSTiQ96C86
MaxQBiQ96C86
PaxDbiQ96C86
PeptideAtlasiQ96C86
PRIDEiQ96C86
ProteomicsDBi76164

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
28960
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
28960
DisGeNETi28960

GeneCards: human genes, protein and diseases

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GeneCardsi
DCPS
HGNCiHGNC:29812 DCPS
HPAiHPA039632
HPA058597
MalaCardsiDCPS
MIMi610534 gene
616459 phenotype
neXtProtiNX_Q96C86
OpenTargetsiENSG00000110063
Orphaneti88616 Autosomal recessive non-syndromic intellectual disability
PharmGKBiPA134863866

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3969 Eukaryota
COG5075 LUCA
GeneTreeiENSGT00390000003924
HOGENOMiHOG000182411
InParanoidiQ96C86
KOiK12584
OMAiIWCEKSH
OrthoDBi930557at2759
PhylomeDBiQ96C86
TreeFamiTF105622

Enzyme and pathway databases

BRENDAi3.6.1.59 2681
ReactomeiR-HSA-429958 mRNA decay by 3' to 5' exoribonuclease

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
DCPS human
EvolutionaryTraceiQ96C86

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
DCPS_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
28960

Protein Ontology

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PROi
PR:Q96C86

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000110063 Expressed in 191 organ(s), highest expression level in liver
GenevisibleiQ96C86 HS

Family and domain databases

Gene3Di3.30.200.40, 1 hit
3.30.428.10, 1 hit
InterProiView protein in InterPro
IPR008594 DcpS/DCS2
IPR019808 Histidine_triad_CS
IPR036265 HIT-like_sf
IPR011145 Scavenger_mRNA_decap_enz_N
PANTHERiPTHR12978 PTHR12978, 1 hit
PfamiView protein in Pfam
PF05652 DcpS, 1 hit
PIRSFiPIRSF028973 Scavenger_mRNA_decap_enz, 1 hit
SUPFAMiSSF102860 SSF102860, 1 hit
SSF54197 SSF54197, 1 hit
PROSITEiView protein in PROSITE
PS00892 HIT_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDCPS_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96C86
Secondary accession number(s): Q8NHL8, Q9Y2S5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 17, 2006
Last modified: May 8, 2019
This is version 158 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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