DCPS

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'-end (N⁷-methyl 5'-triphosphoguanosine)-(purine-ribonucleoside) in mRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
a 5'-end diphospho-(purine-ribonucleoside) in mRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 2
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁷-methyl-GMP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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, ACTIVITY REGULATION.
- Ref.26
  "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, ACTIVITY REGULATION.
EC:
3.6.1.59
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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, ACTIVITY REGULATION.
- Ref.26
  "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, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 5'-end (N⁷-methyl 5'-triphosphoguanosine)-(purine-ribonucleoside) in mRNA
a 5'-(N⁷-methyl 5'-triphosphoguanosine)-(purine-ribonucleoside) residue
zoom
+
H₂O
=
a 5'-end diphospho-(purine-ribonucleoside) in mRNA
a 5'-diphospho-(purine-ribonucleoside) residue
zoom
+
2
H⁺
+
N⁷-methyl-GMP
zoom

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	175	Substrate2 Publications	1
Binding siteⁱ	185	Substrate2 Publications	1
Binding siteⁱ	205	Substrate2 Publications	1
Binding siteⁱ	207	Substrate2 Publications	1
Active siteⁱ	277	Nucleophile	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	mRNA processing, mRNA splicing

Enzyme and pathway databases

BRENDAⁱ	3.6.1.59, 2681
PathwayCommonsⁱ	Q96C86
Reactomeⁱ	R-HSA-429958, 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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000110063.8
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:29812, DCPS
MIMⁱ	610534, gene
neXtProtⁱ	NX_Q96C86

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_073956	316	T → M in ARS; results in a severe decrease of decapase activity. 1 PublicationCorresponds to variant dbSNP:rs137941190EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10 – 13	Missing : Increases cytoplasmic localization. 1 Publication	4
Mutagenesisⁱ	58	R → A: Increases decapping activity to 125% of wild-type. 1 Publication	1
Mutagenesisⁱ	61	I → A: No effect. 1 Publication	1
Mutagenesisⁱ	63	F → A: No effect. 1 Publication	1
Mutagenesisⁱ	83	I → A: Strongly reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	85	E → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	108	F → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	110	N → A: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	113	Y → A: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	128	K → A: No effect. 1 Publication	1
Mutagenesisⁱ	138	K → D: Increases decapping activity to 250% of wild-type. 1 Publication	1
Mutagenesisⁱ	145	R → A: Increases decapping activity to 180% of wild-type. 1 Publication	1
Mutagenesisⁱ	146	Q → P: Increases decapping activity to 140% of wild-type. 1 Publication	1
Mutagenesisⁱ	148	L → A: Inhibits nuclear export to the cytoplasm. 1 Publication	1
Mutagenesisⁱ	150	L → A: Inhibits nuclear export to the cytoplasm. 1 Publication	1
Mutagenesisⁱ	175	W → A: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	185	E → A: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	204	P → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	205	D → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	206	L → A: No effect. 1 Publication	1
Mutagenesisⁱ	207	K → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	207	K → R: No effect. 1 Publication	1
Mutagenesisⁱ	217	Y → A: No effect. 1 Publication	1
Mutagenesisⁱ	217	Y → F: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	268	H → N: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	272	S → A: No effect. 1 Publication	1
Mutagenesisⁱ	273	Y → A: Reduces decapping activity. 1 Publication	1
Mutagenesisⁱ	273	Y → F: Activates decapping activity to 120% of wild-type. 1 Publication	1
Mutagenesisⁱ	277	H → 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	1
Mutagenesisⁱ	279	H → N: Loss of decapping activity. 1 Publication	1
Mutagenesisⁱ	294	R → A or K: No effect. 1 Publication	1
Mutagenesisⁱ	322	R → A: No effect. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	28960
MalaCards human disease database More...MalaCardsⁱ	DCPS
MIMⁱ	616459, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000110063
Orphanetⁱ	88616, Autosomal recessive non-syndromic intellectual disability
PharmGKBⁱ	PA134863866

Miscellaneous databases

Pharosⁱ	Q96C86, Tbio

Pharosⁱ

Q96C86, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL1949488
Drug and drug target database More...DrugBankⁱ	DB07644, 5-[(1S)-1-(3-chlorophenyl)ethoxy]quinazoline-2,4-diamine DB07643, 5-{[1-(2,3-dichlorobenzyl)piperidin-4-yl]methoxy}quinazoline-2,4-diamine DB07642, 5-{[1-(2-fluorobenzyl)piperidin-4-yl]methoxy}quinazoline-2,4-diamine DB03593, 7-methyl-5'-guanylic acid DB01960, 7-methyl-7,8-dihydroguanosine-5'-diphosphate DB01649, 7-methyl-GpppA DB03958, 7-methyl-guanosine-5'-triphosphate-5'-guanosine

Polymorphism and mutation databases

BioMutaⁱ	DCPS
DMDMⁱ	116241325

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources1 Publication
ChainⁱPRO_0000109794	2 – 337	m7GpppX diphosphataseAdd BLAST		336

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources1 Publication	1
Modified residueⁱ	24	PhosphoserineCombined sources	1
Modified residueⁱ	101	PhosphoserineBy similarity	1
Modified residueⁱ	138	N6-acetyllysineCombined sources	1
Modified residueⁱ	142	N6-acetyllysineCombined sources	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q96C86
jPOSTⁱ	Q96C86
MassIVEⁱ	Q96C86
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q96C86
PaxDbⁱ	Q96C86
PeptideAtlas More...PeptideAtlasⁱ	Q96C86
PRIDEⁱ	Q96C86
ProteomicsDBⁱ	76164

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00335385

REPRODUCTION-2DPAGEⁱ

IPI00335385

PTM databases

iPTMnetⁱ	Q96C86
PhosphoSitePlusⁱ	Q96C86

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

Bgeeⁱ	ENSG00000110063, Expressed in right lobe of liver and 204 other tissues
ExpressionAtlasⁱ	Q96C86, baseline and differential
Genevisibleⁱ	Q96C86, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000110063, Low tissue specificity

HPAⁱ

ENSG00000110063, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

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

Interacts with NDOR1.

6 Publications

Binary interactionsⁱ

Hide details

Q96C86

With	#Exp.	IntAct
itself	3	EBI-3917181,EBI-3917181
KPNA2 [P52292]	3	EBI-3917181,EBI-349938
KPNA6 [O60684]	5	EBI-3917181,EBI-359923

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- "A reference map of the human binary protein interactome."
  Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.
  Calderwood M.A.
  Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	118787, 379 interactors
IntActⁱ	Q96C86, 7 interactors
STRINGⁱ	9606.ENSP00000263579

Chemistry databases

BindingDBⁱ

Q96C86

Miscellaneous databases

RNActⁱ	Q96C86, protein

RNActⁱ

Q96C86, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	43 – 45	Combined sources	3
Beta strandⁱ	48 – 56	Combined sources	9
Turnⁱ	57 – 60	Combined sources	4
Beta strandⁱ	61 – 67	Combined sources	7
Beta strandⁱ	79 – 86	Combined sources	8
Helixⁱ	91 – 98	Combined sources	8
Beta strandⁱ	103 – 110	Combined sources	8
Beta strandⁱ	113 – 119	Combined sources	7
Helixⁱ	122 – 124	Combined sources	3
Beta strandⁱ	127 – 132	Combined sources	6
Helixⁱ	137 – 143	Combined sources	7
Beta strandⁱ	148 – 153	Combined sources	6
Helixⁱ	155 – 160	Combined sources	6
Helixⁱ	162 – 167	Combined sources	6
Helixⁱ	174 – 180	Combined sources	7
Beta strandⁱ	183 – 185	Combined sources	3
Helixⁱ	186 – 188	Combined sources	3
Beta strandⁱ	191 – 193	Combined sources	3
Turnⁱ	196 – 198	Combined sources	3
Beta strandⁱ	200 – 204	Combined sources	5
Helixⁱ	213 – 215	Combined sources	3
Beta strandⁱ	217 – 225	Combined sources	9
Helixⁱ	230 – 232	Combined sources	3
Helixⁱ	235 – 237	Combined sources	3
Helixⁱ	238 – 256	Combined sources	19
Helixⁱ	260 – 262	Combined sources	3
Beta strandⁱ	263 – 270	Combined sources	8
Beta strandⁱ	272 – 275	Combined sources	4
Beta strandⁱ	277 – 282	Combined sources	6
Turnⁱ	292 – 294	Combined sources	3
Beta strandⁱ	295 – 297	Combined sources	3
Helixⁱ	298 – 307	Combined sources	10
Helixⁱ	311 – 314	Combined sources	4
Beta strandⁱ	317 – 322	Combined sources	6
Helixⁱ	326 – 333	Combined sources	8

Show more details

3D structure databases

SMRⁱ	Q96C86
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q96C86

EvolutionaryTraceⁱ

Q96C86

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	268 – 279	Substrate bindingAdd BLAST		12

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	10 – 13	nuclear localization signal (NLS)	4
Motifⁱ	142 – 154	nuclear export sequence (NES)Add BLAST	13
Motifⁱ	275 – 279	Histidine triad motif	5

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

eggNOGⁱ	KOG3969, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000003924
HOGENOMⁱ	CLU_041045_2_0_1
InParanoidⁱ	Q96C86
OMAⁱ	FHIHVVN
Database of Orthologous Groups More...OrthoDBⁱ	930557at2759
PhylomeDBⁱ	Q96C86
TreeFamⁱ	TF105622

Family and domain databases

Gene3Dⁱ	3.30.200.40, 1 hit 3.30.428.10, 1 hit
InterProⁱ	View protein in InterPro IPR008594, DcpS/DCS2 IPR019808, Histidine_triad_CS IPR036265, HIT-like_sf IPR011145, Scavenger_mRNA_decap_enz_N
PANTHERⁱ	PTHR12978, PTHR12978, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05652, DcpS, 1 hit
PIRSFⁱ	PIRSF028973, Scavenger_mRNA_decap_enz, 1 hit
SUPFAMⁱ	SSF102860, SSF102860, 1 hit SSF54197, SSF54197, 1 hit
PROSITEⁱ	View protein in PROSITE PS00892, HIT_1, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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 all Align All

Q96C86-1 [UniParc]FASTA Add 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

Checksum:ⁱC9C5A33C212D7A52

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A3B3ITF0	A0A3B3ITF0_HUMAN		DCS-1 DCS-1, EC 3.6.1.59 (Decapping scavenger enzyme) (Hint-related 7meGMP-directed hydrolase) (Histidine triad nucleotide-binding protein 5) (Histidine triad protein member 5) (Scavenger mRNA-decapping enzyme DcpS) (m7GpppX diphosphatase)	DCPS	244	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	69	N → K in AAK91763 (Ref. 1) Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_027958	73	G → E1 PublicationCorresponds to variant dbSNP:rs11557735Ensembl.		1
Natural variantⁱVAR_073956	316	T → M in ARS; results in a severe decrease of decapase activity. 1 PublicationCorresponds to variant dbSNP:rs137941190EnsemblClinVar.		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS8473.1
NCBI Reference Sequences More...RefSeqⁱ	NP_054745.1, NM_014026.4

Genome annotation databases

Ensemblⁱ	ENST00000263579; ENSP00000263579; ENSG00000110063
GeneIDⁱ	28960
KEGGⁱ	hsa:28960
UCSC genome browser More...UCSCⁱ	uc001qdp.3, human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q96C86	m7GpppX diphosphatase		HUMAN		337	UniRef100_Q96C86
+1

Protein	Similar proteins		Species	Score	Length	Source
Q96C86	m7GpppX diphosphatase		HUMAN		337	UniRef90_Q96C86
m7GpppX diphosphatase		PANTR		344
m7GpppX diphosphatase		PROCO		339
m7GpppX diphosphatase		PONAB		337
m7GpppX diphosphatase		PANPA		337
+15

Protein	Similar proteins		Species	Score	Length	Source
Q96C86	m7GpppX diphosphatase	)	MOUSE		338	UniRef50_Q96C86
m7GpppX diphosphatase		RAT		336
m7GpppX diphosphatase		HUMAN		337
m7GpppX diphosphatase		PANTR		344
m7GpppX diphosphatase		PROCO		339
+166

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
CCDSⁱ	CCDS8473.1
RefSeqⁱ	NP_054745.1, NM_014026.4

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4QDE	X-ray	2.90	A/B/C/D	2-337	[»]
	4QDV	X-ray	2.80	A/B/C/D	2-337	[»]
	4QEB	X-ray	3.21	A/B/C/D	2-337	[»]
	5OSY	X-ray	2.06	A/B	37-337	[»]
SMRⁱ	Q96C86
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	118787, 379 interactors
IntActⁱ	Q96C86, 7 interactors
STRINGⁱ	9606.ENSP00000263579

Chemistry databases

BindingDBⁱ	Q96C86
ChEMBLⁱ	CHEMBL1949488
DrugBankⁱ	DB07644, 5-[(1S)-1-(3-chlorophenyl)ethoxy]quinazoline-2,4-diamine DB07643, 5-{[1-(2,3-dichlorobenzyl)piperidin-4-yl]methoxy}quinazoline-2,4-diamine DB07642, 5-{[1-(2-fluorobenzyl)piperidin-4-yl]methoxy}quinazoline-2,4-diamine DB03593, 7-methyl-5'-guanylic acid DB01960, 7-methyl-7,8-dihydroguanosine-5'-diphosphate DB01649, 7-methyl-GpppA DB03958, 7-methyl-guanosine-5'-triphosphate-5'-guanosine

PTM databases

iPTMnetⁱ	Q96C86
PhosphoSitePlusⁱ	Q96C86

Polymorphism and mutation databases

BioMutaⁱ	DCPS
DMDMⁱ	116241325

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00335385

REPRODUCTION-2DPAGEⁱ

IPI00335385

Proteomic databases

EPDⁱ	Q96C86
jPOSTⁱ	Q96C86
MassIVEⁱ	Q96C86
MaxQBⁱ	Q96C86
PaxDbⁱ	Q96C86
PeptideAtlasⁱ	Q96C86
PRIDEⁱ	Q96C86
ProteomicsDBⁱ	76164

Protocols and materials databases

Antibodypediaⁱ	32998, 218 antibodies
The DNASU plasmid repository More...DNASUⁱ	28960

Genome annotation databases

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

Organism-specific databases

CTDⁱ	28960
DisGeNETⁱ	28960
EuPathDBⁱ	HostDB:ENSG00000110063.8
GeneCardsⁱ	DCPS
HGNCⁱ	HGNC:29812, DCPS
HPAⁱ	ENSG00000110063, Low tissue specificity
MalaCardsⁱ	DCPS
MIMⁱ	610534, gene 616459, phenotype
neXtProtⁱ	NX_Q96C86
OpenTargetsⁱ	ENSG00000110063
Orphanetⁱ	88616, Autosomal recessive non-syndromic intellectual disability
PharmGKBⁱ	PA134863866
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3969, Eukaryota
GeneTreeⁱ	ENSGT00390000003924
HOGENOMⁱ	CLU_041045_2_0_1
InParanoidⁱ	Q96C86
OMAⁱ	FHIHVVN
OrthoDBⁱ	930557at2759
PhylomeDBⁱ	Q96C86
TreeFamⁱ	TF105622

Enzyme and pathway databases

BRENDAⁱ	3.6.1.59, 2681
PathwayCommonsⁱ	Q96C86
Reactomeⁱ	R-HSA-429958, mRNA decay by 3' to 5' exoribonuclease

Miscellaneous databases

BioGRID-ORCSⁱ	28960, 212 hits in 854 CRISPR screens
ChiTaRSⁱ	DCPS, human
EvolutionaryTraceⁱ	Q96C86
GeneWikiⁱ	DCPS_(gene)
GenomeRNAiⁱ	28960
Pharosⁱ	Q96C86, Tbio
Protein Ontology More...PROⁱ	PR:Q96C86
RNActⁱ	Q96C86, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000110063, Expressed in right lobe of liver and 204 other tissues
ExpressionAtlasⁱ	Q96C86, baseline and differential
Genevisibleⁱ	Q96C86, HS

Family and domain databases

Gene3Dⁱ	3.30.200.40, 1 hit 3.30.428.10, 1 hit
InterProⁱ	View protein in InterPro IPR008594, DcpS/DCS2 IPR019808, Histidine_triad_CS IPR036265, HIT-like_sf IPR011145, Scavenger_mRNA_decap_enz_N
PANTHERⁱ	PTHR12978, PTHR12978, 1 hit
Pfamⁱ	View protein in Pfam PF05652, DcpS, 1 hit
PIRSFⁱ	PIRSF028973, Scavenger_mRNA_decap_enz, 1 hit
SUPFAMⁱ	SSF102860, SSF102860, 1 hit SSF54197, SSF54197, 1 hit
PROSITEⁱ	View protein in PROSITE PS00892, HIT_1, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DCPS_HUMAN
Accessionⁱ	Q96C86Primary (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:	December 2, 2020
	This is version 169 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Direct protein sequencing, Reference proteome

Documents

Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

UniProtKB

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UniProtKB - Q96C86 (DCPS_HUMAN)

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m7GpppX diphosphatase

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<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

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GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

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Nucleus

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Keywords - Cellular componenti

<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

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

Q96C86

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

Motif

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ